2bw2: Difference between revisions
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New page: left|200px<br /><applet load="2bw2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bw2" /> '''BOFC FROM BACILLUS SUBTILIS'''<br /> ==Over... |
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[[Image:2bw2.gif|left|200px]]<br /><applet load="2bw2" size=" | [[Image:2bw2.gif|left|200px]]<br /><applet load="2bw2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''BOFC FROM BACILLUS SUBTILIS'''<br /> | '''BOFC FROM BACILLUS SUBTILIS'''<br /> | ||
==Overview== | ==Overview== | ||
Sporulation in Bacillus subtilis begins with an asymmetric cell division | Sporulation in Bacillus subtilis begins with an asymmetric cell division giving rise to smaller forespore and larger mother cell compartments. Different programs of gene expression are subsequently directed by compartment-specific RNA polymerase sigma-factors. In the final stages, spore coat proteins are synthesized in the mother cell under the control of RNA polymerase containing sigma(K), (Esigma(K)). sigma(K) is synthesized as an inactive zymogen, pro-sigma(K), which is activated by proteolytic cleavage. Processing of pro-sigma(K) is performed by SpoIVFB, a metalloprotease that resides in a complex with SpoIVFA and bypass of forespore (Bof)A in the outer forespore membrane. Ensuring coordination of events taking place in the two compartments, pro-sigma(K) processing in the mother cell is delayed until appropriate signals are received from the forespore. Cell-cell signaling is mediated by SpoIVB and BofC, which are expressed in the forespore and secreted to the intercompartmental space where they regulate pro-sigma(K) processing by mechanisms that are not yet fully understood. Here we present the three-dimensional structure of BofC determined by solution state NMR. BofC is a monomer made up of two domains. The N-terminal domain, containing a four-stranded beta-sheet onto one face of which an alpha-helix is packed, closely resembles the third immunoglobulin-binding domain of protein G from Streptococcus. The C-terminal domain contains a three-stranded beta-sheet and three alpha-helices in a novel domain topology. The sequence connecting the domains contains a conserved DISP motif to which mutations that affect BofC activity map. Possible roles for BofC in the sigma(K) checkpoint are discussed in the light of sequence and structure comparisons. | ||
==About this Structure== | ==About this Structure== | ||
2BW2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | 2BW2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BW2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ab, E.]] | [[Category: Ab, E.]] | ||
[[Category: Brannigan, J | [[Category: Brannigan, J A.]] | ||
[[Category: Cutting, S | [[Category: Cutting, S M.]] | ||
[[Category: Diercks, T.]] | [[Category: Diercks, T.]] | ||
[[Category: Folkers, G | [[Category: Folkers, G E.]] | ||
[[Category: Jong, R | [[Category: Jong, R N.De.]] | ||
[[Category: Kaptein, R.]] | [[Category: Kaptein, R.]] | ||
[[Category: Patterson, H | [[Category: Patterson, H M.]] | ||
[[Category: Truffault, V.]] | [[Category: Truffault, V.]] | ||
[[Category: Wilkinson, A | [[Category: Wilkinson, A J.]] | ||
[[Category: Wilson, K | [[Category: Wilson, K S.]] | ||
[[Category: bofc]] | [[Category: bofc]] | ||
[[Category: sigmak checkpoint]] | [[Category: sigmak checkpoint]] | ||
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[[Category: sporulation]] | [[Category: sporulation]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:14 2008'' | ||