1re5: Difference between revisions

Revision as of 14:24, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1re5.png

Template:STRUCTURE 1re5

Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putidaCrystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida

Template:ABSTRACT PUBMED 15301541

About this StructureAbout this Structure

1RE5 is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: enzyme evolution in parallel pathways., Yang J, Wang Y, Woolridge EM, Arora V, Petsko GA, Kozarich JW, Ringe D, Biochemistry. 2004 Aug 17;43(32):10424-34. PMID:15301541

Page seeded by OCA on Mon Jul 28 14:24:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1re5.gif|left|200px]]
+{{Seed}}
+[[Image:1re5.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1re5|  PDB=1re5  |  SCENE=  }}
-'''Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida'''
+===Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida===
-==Overview==
+<!--
--Carboxy-cis,cis-muconate lactonizing enzymes (CMLEs), the key enzymes in the protocatechuate branch of the beta-ketoadipate pathway in microorganisms, catalyze the conversion of 3-carboxy-cis,cis-muconate to muconolactones. We have determined the crystal structure of the prokaryotic Pseudomonas putida CMLE (PpCMLE) at 2.6 A resolution. PpCMLE is a homotetramer and belongs to the fumarase class II superfamily. The active site of PpCMLE is formed largely by three regions, which are moderately conserved in the fumarase class II superfamily, from three respective monomers. It has been proposed that residue His141, which is highly conserved in all fumarase class II enzymes and forms a charge relay with residue Glu275 (both His141 and Glu275 are in adenylosuccinate lyase numbering), acts as the general base in most fumarase class II superfamily members. However, this charge relay pair is broken in PpCMLE. The residues corresponding to His141 and Glu275 are Trp153 and Ala289, respectively, in PpCMLE. The structures of prokaryotic MLEs and that of CMLE from the eukaryotic Neurospora crassa are completely different from that of PpCMLE, indicating MLEs and CMLEs, as well as the prokaryotic and eukaryotic CMLEs, evolved from distinct ancestors, although they catalyze similar reactions. The structural differences may be related to recognition by substrates and to differences in the mechanistic pathways by which these enzymes catalyze their respective reactions.
+The line below this paragraph, {{ABSTRACT_PUBMED_15301541}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15301541 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15301541}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Homotetramer]]
 [[Category: Molecular evolution]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:23:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:24:17 2008''