1ozh: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1ozh.gif|left|200px]]
{{Seed}}
[[Image:1ozh.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ozh|  PDB=1ozh  |  SCENE=  }}  
{{STRUCTURE_1ozh|  PDB=1ozh  |  SCENE=  }}  


'''The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.'''
===The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.===




==Overview==
<!--  
Acetohydroxyacid synthase (AHAS) and acetolactate synthase (ALS) are thiamine diphosphate (ThDP)-dependent enzymes that catalyze the decarboxylation of pyruvate to give a cofactor-bound hydroxyethyl group, which is transferred to a second molecule of pyruvate to give 2-acetolactate. AHAS is found in plants, fungi, and bacteria, is involved in the biosynthesis of the branched-chain amino acids, and contains non-catalytic FAD. ALS is found only in some bacteria, is a catabolic enzyme required for the butanediol fermentation, and does not contain FAD. Here we report the 2.3-A crystal structure of Klebsiella pneumoniae ALS. The overall structure is similar to AHAS except for a groove that accommodates FAD in AHAS, which is filled with amino acid side chains in ALS. The ThDP cofactor has an unusual conformation that is unprecedented among the 26 known three-dimensional structures of nine ThDP-dependent enzymes, including AHAS. This conformation suggests a novel mechanism for ALS. A second structure, at 2.0 A, is described in which the enzyme is trapped halfway through the catalytic cycle so that it contains the hydroxyethyl intermediate bound to ThDP. The cofactor has a tricyclic structure that has not been observed previously in any ThDP-dependent enzyme, although similar structures are well known for free thiamine. This structure is consistent with our proposed mechanism and probably results from an intramolecular proton transfer within a tricyclic carbanion that is the true reaction intermediate. Modeling of the second molecule of pyruvate into the active site of the enzyme with the bound intermediate is consistent with the stereochemistry and specificity of ALS.
The line below this paragraph, {{ABSTRACT_PUBMED_14557277}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 14557277 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_14557277}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Acetolactate synthase]]
[[Category: Acetolactate synthase]]
[[Category: Thiamin diphosphate]]
[[Category: Thiamin diphosphate]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:28:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:55:31 2008''

Revision as of 05:55, 29 July 2008

File:1ozh.png

Template:STRUCTURE 1ozh

The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.

Template:ABSTRACT PUBMED 14557277

About this Structure

1OZH is a Single protein structure of sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA.

Reference

The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate., Pang SS, Duggleby RG, Schowen RL, Guddat LW, J Biol Chem. 2004 Jan 16;279(3):2242-53. Epub 2003 Oct 13. PMID:14557277

Page seeded by OCA on Tue Jul 29 08:55:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1ozh&oldid=735520"