198:
results from site-directed mutagenesis studies and not yet experimentally verified. More recently, an X-ray crystal structure on the truncated N-terminal domain revealed crystallographic evidence of two binding sites in the N-terminal domain. These binding sites are at residues 7,37,39 and 76 as well as at residues 36,77, and 79, which agree with the mutagenesis experiments. However, if the N-terminal domain can bind two Ca2+ then either only the N-terminal domain binds calcium, or, the full
Protein S can bind more than two mol of calcium per mol of protein. Since both these claims have been experimentally shown to not be true then the exact binding site of Protein S cannot yet fully be described.
80:
22:
197:
replacements to residue 40 or residue 129 can reduce the binding affinity. Since then, an NMR structure determine positions for the two binding sites at residues 10 and 71 and also at residues 99 and 159. However, these binding sites were based on a cluster analysis of side-chain oxygen atoms and on
137:. Its name derives from being the "S" band in an alphabetical ordering of proteins run from Myxococcus xanthus cell contents on a SDS-denaturing gel. Its study was initially prompted by the huge increase in Protein S production during sporulation of
157:
Protein S is not essential for spore variability and resistance: protein S-deficient spores are viable and are as resistant to heat and sonication as complete spores; glycerol spores lack protein S but are resistant to sonication and
193:
Protein S binds two 2 mol of calcium per mol of protein with a binding dissociation constant of 27 and 76 ΞM according to dialysis experiments. In the same study mutagenesis experiments revealed
546:
Wenk M, Baumgartner R, Holak TA, Huber R, Jaenicke R, Mayr EM (March 1999). "The domains of protein S from
Myxococcus xanthus: structure, stability and interactions".
218:
Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M (February 1994). "NMR-derived three-dimensional solution structure of protein S complexed with calcium".
153:
higher resistance to endure heating, desiccation, UV radiation and sonication no such evidence exists. The work that cites claims no such evidence:
412:
Downard JS, Kupfer D, Zusman DR (June 1984). "Gene expression during development of
Myxococcus xanthus. Analysis of the genes for protein S".
103:
253:
Inouye M, Inouye S, Zusman DR (February 1979). "Gene expression during development of
Myxococcus xanthus: pattern of protein synthesis".
355:"Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens"
507:"Characterization of calcium-binding sites in development-specific protein S of Myxococcus xanthus using site-specific mutagenesis"
182:
587:
168:
and there are other studies that also found that there is no increase in resistance when
Protein S is eliminated.
449:"Myxococcus xanthus spore coat protein S may have a similar structure to vertebrate lens beta gamma-crystallins"
460:
366:
304:
116:
51:
293:"Biosynthesis and self-assembly of protein S, a development-specific protein of Myxococcus xanthus"
32:
484:
150:
138:
133:
563:
528:
476:
429:
394:
332:
270:
235:
555:
518:
468:
421:
384:
374:
322:
312:
262:
227:
181:
Protein S is structured into two domains. The two domains are highly homologous and have a
464:
370:
308:
523:
506:
327:
292:
231:
149:
Though it has been purported as recently as 1994 that
Protein S enables myxospores of
581:
425:
389:
354:
266:
108:
488:
359:
Proceedings of the
National Academy of Sciences of the United States of America
297:
Proceedings of the
National Academy of Sciences of the United States of America
185:
structure. The domains share high similarity with other crystallin proteins.
379:
41:
567:
559:
21:
532:
480:
433:
398:
317:
239:
112:
79:
336:
274:
194:
128:
472:
448:
15:
353:
Bagby S, Harvey TS, Eagle SG, Inouye S, Ikura M (May 1994).
46:
36:
102:
94:
89:
72:
155:
505:Teintze M, Inouye M, Inouye S (January 1988).
348:
346:
291:Inouye M, Inouye S, Zusman DR (January 1979).
286:
284:
8:
500:
498:
213:
211:
78:
522:
388:
378:
326:
316:
447:Wistow G, Summers L, Blundell T (1985).
207:
69:
7:
511:The Journal of Biological Chemistry
14:
20:
1:
524:10.1016/S0021-9258(19)57286-6
232:10.1016/s0969-2126(00)00013-7
548:Journal of Molecular Biology
426:10.1016/0022-2836(84)90180-3
414:Journal of Molecular Biology
267:10.1016/0012-1606(79)90228-8
604:
77:
380:10.1073/pnas.91.10.4308
84:Structure of Protein S.
35:, as no other articles
560:10.1006/jmbi.1999.2582
166:
318:10.1073/pnas.76.1.209
255:Developmental Biology
465:1985Natur.315..771W
371:1994PNAS...91.4308B
309:1979PNAS...76..209I
588:Bacterial proteins
151:Myxococcus xanthus
139:Myxococcus xanthus
134:Myxococcus xanthus
54:for suggestions.
44:to this page from
122:
121:
68:
67:
595:
572:
571:
543:
537:
536:
526:
502:
493:
492:
473:10.1038/315771a0
444:
438:
437:
409:
403:
402:
392:
382:
350:
341:
340:
330:
320:
288:
279:
278:
250:
244:
243:
215:
164:
82:
70:
63:
60:
49:
47:related articles
24:
16:
603:
602:
598:
597:
596:
594:
593:
592:
578:
577:
576:
575:
545:
544:
540:
517:(3): 1199â203.
504:
503:
496:
459:(6022): 771â3.
446:
445:
441:
411:
410:
406:
365:(10): 4308â12.
352:
351:
344:
290:
289:
282:
252:
251:
247:
217:
216:
209:
204:
191:
179:
174:
165:
162:
147:
85:
64:
58:
55:
45:
42:introduce links
25:
12:
11:
5:
601:
599:
591:
590:
580:
579:
574:
573:
554:(5): 1533â45.
538:
494:
439:
404:
342:
280:
245:
206:
205:
203:
200:
190:
187:
178:
175:
173:
170:
160:
146:
143:
120:
119:
106:
100:
99:
96:
92:
91:
87:
86:
83:
75:
74:
66:
65:
52:Find link tool
28:
26:
19:
13:
10:
9:
6:
4:
3:
2:
600:
589:
586:
585:
583:
569:
565:
561:
557:
553:
549:
542:
539:
534:
530:
525:
520:
516:
512:
508:
501:
499:
495:
490:
486:
482:
478:
474:
470:
466:
462:
458:
454:
450:
443:
440:
435:
431:
427:
423:
420:(4): 469â92.
419:
415:
408:
405:
400:
396:
391:
386:
381:
376:
372:
368:
364:
360:
356:
349:
347:
343:
338:
334:
329:
324:
319:
314:
310:
306:
303:(1): 209â13.
302:
298:
294:
287:
285:
281:
276:
272:
268:
264:
261:(2): 579â91.
260:
256:
249:
246:
241:
237:
233:
229:
226:(2): 107â22.
225:
221:
214:
212:
208:
201:
199:
196:
188:
186:
184:
176:
171:
169:
163:Inoyue et al.
159:
154:
152:
144:
142:
140:
136:
135:
130:
126:
118:
114:
110:
107:
105:
101:
97:
93:
88:
81:
76:
71:
62:
53:
48:
43:
39:
38:
34:
29:This article
27:
23:
18:
17:
551:
547:
541:
514:
510:
456:
452:
442:
417:
413:
407:
362:
358:
300:
296:
258:
254:
248:
223:
219:
192:
189:Binding Site
180:
167:
156:
148:
132:
124:
123:
56:
30:
90:Identifiers
59:August 2017
202:References
50:; try the
37:link to it
220:Structure
183:Greek key
172:Structure
131:found in
125:Protein S
73:Protein S
40:. Please
582:Category
568:10064714
195:arginine
177:Overview
161:â
145:Function
533:3121626
489:4274620
481:3925350
461:Bibcode
434:6204058
399:8183906
367:Bibcode
305:Bibcode
240:8081742
129:protein
566:
531:
487:
479:
453:Nature
432:
397:
387:
337:284334
335:
328:382907
325:
275:108160
273:
238:
117:SUPFAM
95:Symbol
33:orphan
31:is an
485:S2CID
390:43774
127:is a
113:SCOPe
104:SCOP2
564:PMID
529:PMID
477:PMID
430:PMID
395:PMID
333:PMID
271:PMID
236:PMID
158:heat
109:1PRS
556:doi
552:286
519:doi
515:263
469:doi
457:315
422:doi
418:175
385:PMC
375:doi
323:PMC
313:doi
263:doi
228:doi
98:PRS
584::
562:.
550:.
527:.
513:.
509:.
497:^
483:.
475:.
467:.
455:.
451:.
428:.
416:.
393:.
383:.
373:.
363:91
361:.
357:.
345:^
331:.
321:.
311:.
301:76
299:.
295:.
283:^
269:.
259:68
257:.
234:.
222:.
210:^
141:.
115:/
111:/
570:.
558::
535:.
521::
491:.
471::
463::
436:.
424::
401:.
377::
369::
339:.
315::
307::
277:.
265::
242:.
230::
224:2
61:)
57:(
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
