1xyl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1xyl.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1xyl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1xyl| PDB=1xyl | SCENE= }}
{{STRUCTURE_1xyl| PDB=1xyl | SCENE= }}
-
'''THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID'''
+
===THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID===
-
==Overview==
+
<!--
-
The distinct roles of the two magnesium ions essential to the activity of D-xylose isomerase from Streptomyces olivochromogenes were examined. The enzyme-magnesium complex was isolated, and the stoichiometry of cation binding determined by neutron activation analysis to be 2 mol of magnesium per mole of enzyme. A plot of Mg2+ added versus Mg2+ bound to enzyme is consistent with apparent KD values of &lt; or = 0.5-1.0 mM for one Mg2+ and &lt; or = 2-5 mM for the second. A site-directed mutant of D-xylose isomerase was designed to remove the tighter, tetracoordinated magnesium binding site (site 1, Mg-1); Glu180 was replaced with Lys180. The stoichiometry of metal binding to this mutant, E180K, is 1 mol of magnesium per mole of enzyme. Ring-opening assays with 1-thioglucose (H2S released upon ring opening) show E180K catalyzes the opening of the sugar ring at 20% the rate of the wild-type, but E180K does not catalyze isomerization of glucose to fructose. Thus, the magnesium bound to Glu180 is essential for isomerization but not essential for ring opening. The X-ray crystallographic structures of E180K in the absence of magnesium and in the presence and absence of 250 mM glucose were obtained to 1.8-A resolution and refined to R factors of 17.7% and 19.7%, respectively. The wild-type and both E180K structures show no significant structural differences, except the epsilon-amino group of Lys180, which occupies the position usually occupied by the Mg-1.(ABSTRACT TRUNCATED AT 250 WORDS)
+
The line below this paragraph, {{ABSTRACT_PUBMED_7906142}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7906142 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7906142}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Petsko, G A.]]
[[Category: Petsko, G A.]]
[[Category: Ringe, D.]]
[[Category: Ringe, D.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:40:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:09:24 2008''

Revision as of 23:09, 28 July 2008

Image:1xyl.png

Template:STRUCTURE 1xyl

THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID

Template:ABSTRACT PUBMED 7906142

About this Structure

1XYL is a Single protein structure of sequence from Streptomyces olivochromogenes. Full crystallographic information is available from OCA.

Reference

Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid., Allen KN, Lavie A, Glasfeld A, Tanada TN, Gerrity DP, Carlson SC, Farber GK, Petsko GA, Ringe D, Biochemistry. 1994 Feb 15;33(6):1488-94. PMID:7906142

Page seeded by OCA on Tue Jul 29 02:09:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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