1pnt: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1pnt.gif|left|200px]]
{{Seed}}
[[Image:1pnt.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pnt|  PDB=1pnt  |  SCENE=  }}  
{{STRUCTURE_1pnt|  PDB=1pnt  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE AT 2.2 ANGSTROMS RESOLUTION'''
===CRYSTAL STRUCTURE OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE AT 2.2 ANGSTROMS RESOLUTION===




==Overview==
<!--
The first X-ray crystallographic structure of a member of the class of low molecular weight (M(r) 18,000) phosphotyrosyl phosphatases is presented. Bovine heart phosphotyrosyl phosphatase (BHPTP) exemplifies this class and is highly homologous (94% sequence identity) to an isoenzyme known as red cell acid phosphatase that is present throughout human tissues. The high-resolution (2.2-A) crystal structure of BHPTP shows that the enzyme consists of a four-strand central parallel beta sheet with alpha helices packed on both sides in a manner characteristic of a Rossmann fold. A bound phosphate ion defines the active site location in a loop of the first beta alpha beta motif at the C-terminus of the beta sheet. The location and enzymatic significance of the residues in the characteristic low molecular weight PTPase active site motif, including the essential arginine (Arg 18) and nucleophilic cysteine (Cys 12), are described. The functional role of a histidine (His 72) suggested previously to be near the active site is defined in the structure, as well as a potential proton donor for the leaving group in the tyrosyl phosphate cleavage. Surface maps of BHPTP define a hydrophobic crevice suitable for phosphotyrosyl peptide binding. Comparison of the BHPTP structure to the related, but structurally distinct enzyme PTP1B is made, illustrating the unique way this smallest of these phosphatases has formed the phosphotyrosine active site.
The line below this paragraph, {{ABSTRACT_PUBMED_7537084}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7537084 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7537084}}


==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Zhang, M.]]
[[Category: Zhang, M.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:17:20 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:08:57 2008''

Revision as of 06:09, 28 July 2008

File:1pnt.png

Template:STRUCTURE 1pnt

CRYSTAL STRUCTURE OF BOVINE HEART PHOSPHOTYROSYL PHOSPHATASE AT 2.2 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 7537084

About this Structure

1PNT is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-A resolution., Zhang M, Van Etten RL, Stauffacher CV, Biochemistry. 1994 Sep 20;33(37):11097-105. PMID:7537084

Page seeded by OCA on Mon Jul 28 09:08:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1pnt&oldid=691369"