1xg3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xg3.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xg3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xg3| PDB=1xg3 | SCENE= }}
{{STRUCTURE_1xg3| PDB=1xg3 | SCENE= }}
-
'''Crystal structure of the C123S 2-methylisocitrate lyase mutant from Escherichia coli in complex with the reaction product, Mg(II)-pyruvate and succinate'''
+
===Crystal structure of the C123S 2-methylisocitrate lyase mutant from Escherichia coli in complex with the reaction product, Mg(II)-pyruvate and succinate===
-
==Overview==
+
<!--
-
Two crystal structures of the C123S mutant of 2-methylisocitrate lyase have been determined, one with the bound reaction products, Mg(2+)-pyruvate and succinate, and the second with a bound Mg(2+)-(2R,3S)-isocitrate inhibitor. Comparison with the structure of the wild-type enzyme in the unbound state reveals that the enzyme undergoes a conformational transition that sequesters the ligand from solvent, as previously observed for two other enzyme superfamily members, isocitrate lyase and phosphoenolpyruvate mutase. The binding modes reveal the determinants of substrate specificity and stereoselectivity, and the stringent specificity is verified in solution using various potential substrates. A model of bound 2-methylisocitrate has been developed based on the experimentally determined structures. We propose a catalytic mechanism involving an alpha-carboxy-carbanion intermediate/transition state, which is consistent with previous stereochemical experiments showing inversion of configuration at the C(3) of 2-methylisocitrate. Structure-based sequence analysis and phylogenic tree construction reveal determinants of substrate specificity, highlight nodes of divergence of families, and predict enzyme families with new functions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15723538}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15723538 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15723538}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Pyruvate]]
[[Category: Pyruvate]]
[[Category: Succinate]]
[[Category: Succinate]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:59:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:31:17 2008''

Revision as of 06:31, 29 July 2008

Template:STRUCTURE 1xg3

Crystal structure of the C123S 2-methylisocitrate lyase mutant from Escherichia coli in complex with the reaction product, Mg(II)-pyruvate and succinate

Template:ABSTRACT PUBMED 15723538

About this Structure

1XG3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution., Liu S, Lu Z, Han Y, Melamud E, Dunaway-Mariano D, Herzberg O, Biochemistry. 2005 Mar 1;44(8):2949-62. PMID:15723538

Page seeded by OCA on Tue Jul 29 09:31:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools