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.


1y7a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1y7a.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1y7a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1y7a| PDB=1y7a | SCENE= }}
{{STRUCTURE_1y7a| PDB=1y7a | SCENE= }}
-
'''Structure of D153H/K328W E. coli alkaline phosphatase in presence of cobalt at 1.77 A resolution'''
+
===Structure of D153H/K328W E. coli alkaline phosphatase in presence of cobalt at 1.77 A resolution===
-
==Overview==
+
<!--
-
Escherichia coli alkaline phosphatase exhibits maximal activity when Zn(2+) fills the M1 and M2 metal sites and Mg(2+) fills the M3 metal site. When other metals replace the zinc and magnesium, the catalytic efficiency is reduced by more than 5000-fold. Alkaline phosphatases from organisms such as Thermotoga maritima and Bacillus subtilis require cobalt for maximal activity and function poorly with zinc and magnesium. Previous studies have shown that the D153H alkaline phosphatase exhibited very little activity in the presence of cobalt, while the K328W and especially the D153H/K328W mutant enzymes can use cobalt for catalysis. To understand the structural basis for the altered metal specificity and the ability of the D153H/K328W enzyme to utilize cobalt for catalysis, we determined the structures of the inactive wild-type E. coli enzyme with cobalt (WT_Co) and the structure of the active D153H/K328W enzyme with cobalt (HW_Co). The structural data reveal differences in the metal coordination and in the strength of the interaction with the product phosphate (P(i)). Since release of P(i) is the slow step in the mechanism at alkaline pH, the enhanced binding of P(i) in the WT_Co structure explains the observed decrease in activity, while the weakened binding of P(i) in the HW_Co structure explains the observed increase in activity. These alterations in P(i) affinity are directly related to alterations in the coordination of the metals in the active site of the enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15938627}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15938627 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15938627}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Metal specificity]]
[[Category: Metal specificity]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:57:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:36:37 2008''

Revision as of 04:36, 29 July 2008

Image:1y7a.png

Template:STRUCTURE 1y7a

Structure of D153H/K328W E. coli alkaline phosphatase in presence of cobalt at 1.77 A resolution

Template:ABSTRACT PUBMED 15938627

About this Structure

1Y7A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase., Wang J, Stieglitz KA, Kantrowitz ER, Biochemistry. 2005 Jun 14;44(23):8378-86. PMID:15938627

Page seeded by OCA on Tue Jul 29 07:36:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y7a"
Personal tools