This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1s2w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1s2w.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1s2w.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1s2w| PDB=1s2w | SCENE= }}
{{STRUCTURE_1s2w| PDB=1s2w | SCENE= }}
-
'''Crystal structure of phosphoenolpyruvate mutase in high ionic strength'''
+
===Crystal structure of phosphoenolpyruvate mutase in high ionic strength===
-
==Overview==
+
<!--
-
Previous work has indicated that PEP mutase catalyzes the rearrangement of phosphoenolpyruvate to phosphonopyruvate by a dissociative mechanism. The crystal structure of the mutase with Mg(II) and sulfopyruvate (a phosphonopyruvate analogue) bound showed that the substrate is anchored to the active site by the Mg(II), and shielded from solvent by a large loop (residues 115-133). Here, the crystal structures of wild-type and D58A mutases, in the apo state and in complex with Mg(II), are reported. In both unbound and Mg(II)-bound states, the active site is accessible to the solvent. The loop (residues 115-133), which in the enzyme-inhibitor complexes covers the active site cavity, is partially disordered or adopts a conformation that allows access to the cavity. In the apo state, the residues associated with Mg(II) binding are poised to accept the metal ion. When Mg(II) binds, the coordination is the same as that previously observed in the enzyme-Mg(II) sulfopyruvate complex, except that the coordination positions occupied by two ligand oxygen atoms are occupied by two water molecules. When the loop opens, three key active site residues are displaced from the active site, Lys120, Asn122, and Leu124. Lys120 mediates Mg(II) coordination. Asn122 and Leu124 surround the transferring phosphoryl group, and thus prevent substrate hydrolysis. Amino acid replacement of any one of these three loop residues results in a significant loss of catalytic activity. It is hypothesized that the loop serves to gate the mutase active site, interconverting between an open conformation that allows substrate binding and product release and a closed conformation that separates the reaction site from the solvent during catalysis.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15078090}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15078090 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15078090}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Phosphonopyruvate]]
[[Category: Phosphonopyruvate]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:13:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:27:32 2008''

Revision as of 13:27, 28 July 2008

Image:1s2w.png

Template:STRUCTURE 1s2w

Crystal structure of phosphoenolpyruvate mutase in high ionic strength

Template:ABSTRACT PUBMED 15078090

About this Structure

1S2W is a Single protein structure of sequence from Mytilus edulis. Full crystallographic information is available from OCA.

Reference

Conformational flexibility of PEP mutase., Liu S, Lu Z, Han Y, Jia Y, Howard A, Dunaway-Mariano D, Herzberg O, Biochemistry. 2004 Apr 20;43(15):4447-53. PMID:15078090

Page seeded by OCA on Mon Jul 28 16:27:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1s2w"
Personal tools