This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2bw2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2bw2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2bw2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2bw2| PDB=2bw2 | SCENE= }}
{{STRUCTURE_2bw2| PDB=2bw2 | SCENE= }}
-
'''BOFC FROM BACILLUS SUBTILIS'''
+
===BOFC FROM BACILLUS SUBTILIS===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16049010}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16049010 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16049010}}
==About this Structure==
==About this Structure==
-
2BW2 is a [[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].
+
2BW2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BW2 OCA].
==Reference==
==Reference==
Line 37: Line 41:
[[Category: Signaling protein]]
[[Category: Signaling protein]]
[[Category: Sporulation]]
[[Category: Sporulation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:53:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:47:03 2008''

Revision as of 16:47, 27 July 2008

Image:2bw2.png

Template:STRUCTURE 2bw2

BOFC FROM BACILLUS SUBTILIS

Template:ABSTRACT PUBMED 16049010

About this Structure

2BW2 is a Single protein structure of sequence from Bacillus subtilis. Full experimental information is available from OCA.

Reference

The structure of bypass of forespore C, an intercompartmental signaling factor during sporulation in Bacillus., Patterson HM, Brannigan JA, Cutting SM, Wilson KS, Wilkinson AJ, Ab E, Diercks T, de Jong RN, Truffault V, Folkers GE, Kaptein R, J Biol Chem. 2005 Oct 28;280(43):36214-20. Epub 2005 Jul 27. PMID:16049010

Page seeded by OCA on Sun Jul 27 19:47:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bw2"
Personal tools