We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2iuc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2iuc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2iuc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2iuc| PDB=2iuc | SCENE= }}
{{STRUCTURE_2iuc| PDB=2iuc | SCENE= }}
-
'''STRUCTURE OF ALKALINE PHOSPHATASE FROM THE ANTARCTIC BACTERIUM TAB5'''
+
===STRUCTURE OF ALKALINE PHOSPHATASE FROM THE ANTARCTIC BACTERIUM TAB5===
-
==Overview==
+
<!--
-
Alkaline phosphatases (APs) are non-specific phosphohydrolases that are widely used in molecular biology and diagnostics. We describe the structure of the cold active alkaline phosphatase from the Antarctic bacterium TAB5 (TAP). The fold and the active site geometry are conserved with the other AP structures, where the monomer has a large central beta-sheet enclosed by alpha-helices. The dimer interface of TAP is relatively small, and only a single loop from each monomer replaces the typical crown domain. The structure also has typical cold-adapted features; lack of disulfide bridges, low number of salt-bridges, and a loose dimer interface that completely lacks charged interactions. The dimer interface is more hydrophobic than that of the Escherichia coli AP and the interactions have tendency to pair with backbone atoms, which we propose to result from the cold adaptation of TAP. The structure contains two additional magnesium ions outside of the active site, which we believe to be involved in substrate binding as well as contributing to the local stability. The M4 site stabilises an interaction that anchors the substrate-coordinating R148. The M5 metal-binding site is in a region that stabilises metal coordination in the active site. In other APs the M5 binding area is supported by extensive salt-bridge stabilisation, as well as positively charged patches around the active site. We propose that these charges, and the TAP M5 binding, influence the release of the product phosphate and thus might influence the rate-determining step of the enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17198711}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17198711 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17198711}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Psycrophile]]
[[Category: Psycrophile]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:53:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:46:09 2008''

Revision as of 02:46, 28 July 2008

Image:2iuc.png

Template:STRUCTURE 2iuc

STRUCTURE OF ALKALINE PHOSPHATASE FROM THE ANTARCTIC BACTERIUM TAB5

Template:ABSTRACT PUBMED 17198711

About this Structure

2IUC is a Protein complex structure of sequences from Antarctic bacterium tab5. Full crystallographic information is available from OCA.

Reference

Crystal structure of alkaline phosphatase from the Antarctic bacterium TAB5., Wang E, Koutsioulis D, Leiros HK, Andersen OA, Bouriotis V, Hough E, Heikinheimo P, J Mol Biol. 2007 Mar 2;366(4):1318-31. Epub 2006 Dec 2. PMID:17198711

Page seeded by OCA on Mon Jul 28 05:46:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iuc"
Personal tools