1uzl: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1uzl.gif|left|200px]]
{{Seed}}
[[Image:1uzl.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1uzl|  PDB=1uzl  |  SCENE=  }}  
{{STRUCTURE_1uzl|  PDB=1uzl  |  SCENE=  }}  


'''MABA FROM MYCOBACTERIUM TUBERCULOSIS'''
===MABA FROM MYCOBACTERIUM TUBERCULOSIS===




==Overview==
<!--  
The fatty acid elongation system FAS-II is involved in the biosynthesis of mycolic acids, which are major and specific long-chain fatty acids of the cell envelope of Mycobacterium tuberculosis and other mycobacteria, including Mycobacterium smegmatis. The protein MabA, also named FabG1, has been shown recently to be part of FAS-II and to catalyse the NADPH-specific reduction of long chain beta-ketoacyl derivatives. This activity corresponds to the second step of an FAS-II elongation round. FAS-II is inhibited by the antituberculous drug isoniazid through the inhibition of the 2-trans-enoyl-acyl carrier protein reductase InhA. Thus, the other enzymes making up this enzymatic complex represent potential targets for designing new antituberculous drugs. The crystal structure of the apo-form MabA was solved to 2.03 A resolution by molecular replacement. MabA is tetrameric and shares the conserved fold of the short-chain dehydrogenases/reductases (SDRs). However, it exhibits some significant local rearrangements of the active-site loops in the absence of a cofactor, particularly the beta5-alpha5 region carrying the unique tryptophan residue, in agreement with previous fluorescence spectroscopy data. A similar conformation has been observed in the beta-ketoacyl reductase from Escherichia coli and the distantly related dehydratase. The distinctive enzymatic and structural properties of MabA are discussed in view of its crystal structure and that of related enzymes.
The line below this paragraph, {{ABSTRACT_PUBMED_12079383}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12079383 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12079383}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Nadp]]
[[Category: Nadp]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:54:36 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:49:08 2008''

Revision as of 15:49, 27 July 2008

File:1uzl.png

Template:STRUCTURE 1uzl

MABA FROM MYCOBACTERIUM TUBERCULOSIS

Template:ABSTRACT PUBMED 12079383

About this Structure

1UZL is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis., Cohen-Gonsaud M, Ducasse S, Hoh F, Zerbib D, Labesse G, Quemard A, J Mol Biol. 2002 Jul 5;320(2):249-61. PMID:12079383

Page seeded by OCA on Sun Jul 27 18:49:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1uzl&oldid=661524"