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.


1qsp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qsp.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qsp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qsp| PDB=1qsp | SCENE= }}
{{STRUCTURE_1qsp| PDB=1qsp | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE YEAST PHOSPHORELAY PROTEIN YPD1'''
+
===CRYSTAL STRUCTURE OF THE YEAST PHOSPHORELAY PROTEIN YPD1===
-
==Overview==
+
<!--
-
In Saccharomyces cerevisiae, the SLN1-YPD1-SSK1 phosphorelay system controls a downstream mitogen-activated protein (MAP) kinase in response to hyperosmotic stress. YPD1 functions as a phospho-histidine protein intermediate which is required for phosphoryl group transfer from the sensor kinase SLN1 to the response regulator SSK1. In addition, YPD1 mediates phosphoryl transfer from SLN1 to SKN7, the only other response regulator protein in yeast which plays a role in response to oxidative stress and cell wall biosynthesis.The X-ray structure of YPD1 was solved at a resolution of 2.7 A by conventional multiple isomorphous replacement with anomalous scattering. The tertiary structure of YPD1 consists of six alpha-helices and a short 310-helix. A four-helix bundle comprises the central core of the molecule and contains the histidine residue that is phosphorylated. Structure-based comparisons of YPD1 to other proteins having a similar function, such as the Escherichia coli ArcB histidine-containing phosphotransfer (HPt) domain and the P1 domain of the CheA kinase, revealed that the helical bundle and several structural features around the active-site histidine residue are conserved between the prokaryotic and eukaryotic kingdoms.Despite limited amino acid sequence homology among HPt domains, our analysis of YPD1 as a prototypical family member, indicates that these phosphotransfer domains are likely to share a similar fold and common features with regard to response regulator binding and mechanism for histidine-aspartate phosphoryl transfer.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10512701}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10512701 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10512701}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Four-helix bundle]]
[[Category: Four-helix bundle]]
[[Category: Two- component signal transduction]]
[[Category: Two- component signal transduction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:39:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:03:02 2008''

Revision as of 15:03, 27 July 2008

Image:1qsp.png

Template:STRUCTURE 1qsp

CRYSTAL STRUCTURE OF THE YEAST PHOSPHORELAY PROTEIN YPD1

Template:ABSTRACT PUBMED 10512701

About this Structure

1QSP is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Conservation of structure and function among histidine-containing phosphotransfer (HPt) domains as revealed by the crystal structure of YPD1., Xu Q, West AH, J Mol Biol. 1999 Oct 8;292(5):1039-50. PMID:10512701

Page seeded by OCA on Sun Jul 27 18:03:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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