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[[Image:2jol.gif|left|200px]]
{{Seed}}
[[Image:2jol.png|left|200px]]


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{{STRUCTURE_2jol|  PDB=2jol  |  SCENE=  }}  
{{STRUCTURE_2jol|  PDB=2jol  |  SCENE=  }}  


'''Average NMR structure of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei'''
===Average NMR structure of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei===




==Overview==
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BopE is a type III secreted protein from Burkholderia pseudomallei, the aetiological agent of melioidosis, a severe emerging infection. BopE is a GEF (guanine-nucleotide-exchange factor) for the Rho GTPases Cdc42 (cell division cycle 42) and Rac1. We have determined the structure of BopE catalytic domain (amino acids 78-261) by NMR spectroscopy and it shows that BopE(78-261) comprises two three-helix bundles (alpha1alpha4alpha5 and alpha2alpha3alpha6). This fold is similar to that adopted by the BopE homologues SopE and SopE2, which are GEFs from Salmonella. Whereas the two three-helix bundles of SopE(78-240) and SopE2(69-240) form the arms of a 'Lambda' shape, BopE(78-261) adopts a more closed conformation with substantial interactions between the two three-helix bundles. We propose that arginine and proline residues are important in the conformational differences between BopE and SopE/E2. Analysis of the molecular interface in the SopE(78-240)-Cdc42 complex crystal structure indicates that, in a BopE-Cdc42 interaction, the closed conformation of BopE(78-261) would engender steric clashes with the Cdc42 switch regions. This implies that BopE(78-261) must undergo a closed-to-open conformational change in order to catalyse guanine nucleotide exchange. In an NMR titration to investigate the BopE(78-261)-Cdc42 interaction, the appearance of additional peaks per NH for residues in hinge regions of BopE(78-261) indicates that BopE(78-261) does undergo a closed-to-open conformational change in the presence of Cdc42. The conformational change hypothesis is further supported by substantial improvement of BopE(78-261) catalytic efficiency through mutations that favour an open conformation. Requirement for closed-to-open conformational change explains the 10-40-fold lower k(cat) of BopE compared with SopE and SopE2.
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{{ABSTRACT_PUBMED_18052936}}


==About this Structure==
==About this Structure==
2JOL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2aic 2aic]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOL OCA].  
2JOL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2aic 2aic]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JOL OCA].  


==Reference==
==Reference==
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[[Category: Sope2]]
[[Category: Sope2]]
[[Category: Type iii secretion]]
[[Category: Type iii secretion]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:28:08 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:18:05 2008''

Revision as of 13:18, 29 July 2008

File:2jol.png

Template:STRUCTURE 2jol

Average NMR structure of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei

Template:ABSTRACT PUBMED 18052936

About this Structure

2JOL is a Single protein structure of sequence from Burkholderia pseudomallei. This structure supersedes the now removed PDB entry 2aic. Full experimental information is available from OCA.

Reference

The guanine-nucleotide-exchange factor BopE from Burkholderia pseudomallei adopts a compact version of the Salmonella SopE/SopE2 fold and undergoes a closed-to-open conformational change upon interaction with Cdc42., Upadhyay A, Wu HL, Williams C, Field T, Galyov EE, van den Elsen JM, Bagby S, Biochem J. 2008 May 1;411(3):485-93. PMID:18052936

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