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.


1ypt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ypt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ypt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ypt| PDB=1ypt | SCENE= }}
{{STRUCTURE_1ypt| PDB=1ypt | SCENE= }}
-
'''CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE'''
+
===CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE===
-
==Overview==
+
<!--
-
Protein tyrosine phosphatases (PTPases) and kinases coregulate the critical levels of phosphorylation necessary for intracellular signalling, cell growth and differentiation. Yersinia, the causative bacteria of the bubonic plague and other enteric diseases, secrete an active PTPase, Yop51, that enters and suppresses host immune cells. Though the catalytic domain is only approximately 20% identical to human PTP1B, the Yersinia PTPase contains all of the invariant residues present in eukaryotic PTPases, including the nucleophilic Cys 403 which forms a phosphocysteine intermediate during catalysis. We present here structures of the unliganded (2.5 A resolution) and tungstate-bound (2.6 A) crystal forms which reveal that Cys 403 is positioned at the centre of a distinctive phosphate-binding loop. This loop is at the hub of several hydrogen-bond arrays that not only stabilize a bound oxyanion, but may activate Cys 403 as a reactive thiolate. Binding of tungstate triggers a conformational change that traps the oxyanion and swings Asp 356, an important catalytic residue, by approximately 6 A into the active site. The same anion-binding loop in PTPases is also found in the enzyme rhodanese.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8052312}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8052312 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8052312}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Zhang, Z Y.]]
[[Category: Zhang, Z Y.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:37:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:55:31 2008''

Revision as of 04:55, 28 July 2008

Image:1ypt.png

Template:STRUCTURE 1ypt

CRYSTAL STRUCTURE OF YERSINIA PROTEIN TYROSINE PHOSPHATASE AT 2.5 ANGSTROMS AND THE COMPLEX WITH TUNGSTATE

Template:ABSTRACT PUBMED 8052312

About this Structure

1YPT is a Single protein structure of sequence from Yersinia enterocolitica. Full crystallographic information is available from OCA.

Reference

Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate., Stuckey JA, Schubert HL, Fauman EB, Zhang ZY, Dixon JE, Saper MA, Nature. 1994 Aug 18;370(6490):571-5. PMID:8052312

Page seeded by OCA on Mon Jul 28 07:55:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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