4xim

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:4xim.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:4xim.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_4xim| PDB=4xim | SCENE= }}
{{STRUCTURE_4xim| PDB=4xim | SCENE= }}
-
'''PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES'''
+
===PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES===
-
==Overview==
+
<!--
-
The structure and function of the xylose (glucose) isomerase from Actinoplanes missouriensis have been analyzed by X-ray crystallography and site-directed mutagenesis after cloning and overexpression in Escherichia coli. The crystal structure of wild-type enzyme has been refined to an R factor of 15.2% against diffraction data to 2.2-A resolution. The structures of a number of binary and ternary complexes involving wild-type and mutant enzymes, the divalent cations Mg2+, Co2+, or Mn2+, and either the substrate xylose or substrate analogs have also been determined and refined to comparable R factors. Two metal sites are identified. Metal site 1 is four-coordinated and tetrahedral in the absence of substrate and is six-coordinated and octahedral in its presence; the O2 and O4 atoms of linear inhibitors and substrate bind to metal 1. Metal site 2 is octahedral in all cases; its position changes by 0.7 A when it binds O1 of the substrate and by more than 1 A when it also binds O2; these bonds replace bonds to carboxylate ligands from the protein. Side chains involved in metal binding have been substituted by site-directed mutagenesis. The biochemical properties of the mutant enzymes are presented. Together with structural data, they demonstrate that the two metal ions play an essential part in binding substrates, in stabilizing their open form, and in catalyzing hydride transfer between the C1 and C2 positions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1610791}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1610791 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1610791}}
==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Xylose isomerase]]
[[Category: Xylose isomerase]]
[[Category: Janin, J.]]
[[Category: Janin, J.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:31:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:54:50 2008''

Revision as of 10:54, 3 July 2008

Image:4xim.png

Template:STRUCTURE 4xim

PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES

Template:ABSTRACT PUBMED 1610791

About this Structure

4XIM is a Single protein structure of sequence from Actinoplanes missouriensis. Full crystallographic information is available from OCA.

Reference

Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites., Jenkins J, Janin J, Rey F, Chiadmi M, van Tilbeurgh H, Lasters I, De Maeyer M, Van Belle D, Wodak SJ, Lauwereys M, et al., Biochemistry. 1992 Jun 23;31(24):5449-58. PMID:1610791

Page seeded by OCA on Thu Jul 3 13:54:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4xim"
Personal tools