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.


1h73

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1h73.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1h73.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1h73| PDB=1h73 | SCENE= }}
{{STRUCTURE_1h73| PDB=1h73 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH THREONINE'''
+
===CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH THREONINE===
-
==Overview==
+
<!--
-
Homoserine kinase (HSK), the fourth enzyme in the aspartate pathway of amino acid biosynthesis, catalyzes the phosphorylation of L-homoserine (Hse) to L-homoserine phosphate, an intermediate in the production of L-threonine, L-isoleucine, and in higher plants, L-methionine. The high-resolution structures of Methanococcus jannaschii HSK ternary complexes with its amino acid substrate and ATP analogues have been determined by X-ray crystallography. These structures reveal the structural determinants of the tight and highly specific binding of Hse, which is coupled with local conformational changes that enforce the sequestration of the substrate. The delta-hydroxyl group of bound Hse is only 3.4 A away from the gamma-phosphate of the bound nucleotide, poised for the in-line attack at the gamma-phosphorus. The bound nucleotides are flexible at the triphosphate tail. Nevertheless, a Mg(2+) was located in one of the complexes that binds between the beta- and gamma-phosphates of the nucleotide with good ligand geometry and is coordinated by the side chain of Glu130. No strong nucleophile (base) can be located near the phosphoryl acceptor hydroxyl group. Therefore, we propose that the catalytic mechanism of HSK does not involve a catalytic base for activating the phosphoryl acceptor hydroxyl but instead is mediated via a transition state stabilization mechanism.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11535056}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11535056 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11535056}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Threonine biosynthesis]]
[[Category: Threonine biosynthesis]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:31:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:44:03 2008''

Revision as of 03:44, 1 July 2008

Image:1h73.png

Template:STRUCTURE 1h73

CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH THREONINE

Template:ABSTRACT PUBMED 11535056

About this Structure

1H73 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

Structural basis for the catalysis and substrate specificity of homoserine kinase., Krishna SS, Zhou T, Daugherty M, Osterman A, Zhang H, Biochemistry. 2001 Sep 11;40(36):10810-8. PMID:11535056

Page seeded by OCA on Tue Jul 1 06:44:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h73"
Personal tools