2vqg: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Newer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px <!-- The line below this paragraph, containing "STRUCTURE_2vqg", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2vqg.jpg|left|200px]]
{{Seed}}
[[Image:2vqg.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vqg|  PDB=2vqg  |  SCENE=  }}  
{{STRUCTURE_2vqg|  PDB=2vqg  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF PORB FROM CORYNEBACTERIUM GLUTAMICUM (CRYSTAL FORM I)'''
===CRYSTAL STRUCTURE OF PORB FROM CORYNEBACTERIUM GLUTAMICUM (CRYSTAL FORM I)===




==Overview==
<!--
The cell wall of Corynebacterium glutamicum contains a mycolic acid layer, which is a protective nonpolar barrier similar to the outer membrane of Gram-negative bacteria. The exchange of material across this barrier requires porins. Porin B (PorB) is one of them. Recombinant PorB has been produced in Escherichia coli, purified, crystallized and analyzed by X-ray diffraction, yielding 16 independent molecular structures in four different crystal forms at resolutions up to 1.8 A. All 16 molecules have the same globular core, which consists of 70 residues forming four alpha-helices tied together by a disulfide bridge. The 16 structures vary greatly with respect to the 29 residues in the N- and C-terminal extensions. Since corynebacteria belong to the group of mycolata that includes some prominent human pathogens, the observed structure may be of medical relevance. Due to the clearly established solid structure of the core, the native porin has to be oligomeric, and the reported structure is one of the subunits. An alpha-helical porin in a bacterial outer envelope is surprising because all presently known structures of such porins consist of beta-barrels. Since none of the four crystal packing arrangements was compatible with an oligomeric membrane channel, we constructed a model of such an oligomer that was consistent with all available data of native PorB. The proposed model is based on the required polar interior and nonpolar exterior of the porin, on a recurring crystal packing contact around a 2-fold axis, on the assumption of a simple C(n) symmetry (a symmetric arrangement around an n-fold axis), on the experimentally established electric conductivity and anion selectivity and on the generally observed shape of porin channels.
The line below this paragraph, {{ABSTRACT_PUBMED_18462756}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18462756 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18462756}}


==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Transmembrane]]
[[Category: Transmembrane]]
[[Category: Transport]]
[[Category: Transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu May 22 21:42:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:32:58 2008''

Revision as of 22:33, 28 July 2008

File:2vqg.png

Template:STRUCTURE 2vqg

CRYSTAL STRUCTURE OF PORB FROM CORYNEBACTERIUM GLUTAMICUM (CRYSTAL FORM I)

Template:ABSTRACT PUBMED 18462756

About this Structure

2VQG is a Single protein structure of sequence from Corynebacterium glutamicum. Full crystallographic information is available from OCA.

Reference

A Putative alpha-Helical Porin from Corynebacterium glutamicum., Ziegler K, Benz R, Schulz GE, J Mol Biol. 2008 Jun 6;379(3):482-91. Epub 2008 Apr 11. PMID:18462756

Page seeded by OCA on Tue Jul 29 01:32:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2vqg&oldid=722058"