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.


1fwl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fwl.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1fwl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fwl| PDB=1fwl | SCENE= }}
{{STRUCTURE_1fwl| PDB=1fwl | SCENE= }}
-
'''CRYSTAL STRUCTURE OF HOMOSERINE KINASE'''
+
===CRYSTAL STRUCTURE OF HOMOSERINE KINASE===
-
==Overview==
+
<!--
-
BACKGROUND: Homoserine kinase (HSK) catalyzes an important step in the threonine biosynthesis pathway. It belongs to a large yet unique class of small metabolite kinases, the GHMP kinase superfamily. Members in the GHMP superfamily participate in several essential metabolic pathways, such as amino acid biosynthesis, galactose metabolism, and the mevalonate pathway. RESULTS: The crystal structure of HSK and its complex with ADP reveal a novel nucleotide binding fold. The N-terminal domain contains an unusual left-handed betaalphabeta unit, while the C-terminal domain has a central alpha-beta plait fold with an insertion of four helices. The phosphate binding loop in HSK is distinct from the classical P loops found in many ATP/GTP binding proteins. The bound ADP molecule adopts a rare syn conformation and is in the opposite orientation from those bound to the P loop-containing proteins. Inspection of the substrate binding cavity indicates several amino acid residues that are likely to be involved in substrate binding and catalysis. CONCLUSIONS: The crystal structure of HSK is the first representative in the GHMP superfamily to have determined structure. It provides insight into the structure and nucleotide binding mechanism of not only the HSK family but also a variety of enzymes in the GHMP superfamily. Such enzymes include galactokinases, mevalonate kinases, phosphomevalonate kinases, mevalonate pyrophosphate decarboxylases, and several proteins of yet unknown functions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11188689}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11188689 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11188689}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Zhou, T.]]
[[Category: Zhou, T.]]
[[Category: Kinase]]
[[Category: Kinase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:50:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:03:10 2008''

Revision as of 01:03, 1 July 2008

Image:1fwl.png

Template:STRUCTURE 1fwl

CRYSTAL STRUCTURE OF HOMOSERINE KINASE

Template:ABSTRACT PUBMED 11188689

About this Structure

1FWL is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily., Zhou T, Daugherty M, Grishin NV, Osterman AL, Zhang H, Structure. 2000 Dec 15;8(12):1247-57. PMID:11188689

Page seeded by OCA on Tue Jul 1 04:03:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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