2uyt: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:2uyt.gif|left|200px]]
{{Seed}}
[[Image:2uyt.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2uyt|  PDB=2uyt  |  SCENE=  }}  
{{STRUCTURE_2uyt|  PDB=2uyt  |  SCENE=  }}  


'''STRUCTURE OF L-RHAMNULOSE KINASE IN COMPLEX WITH ADP AND BETA-L-RHAMNULOSE.'''
===STRUCTURE OF L-RHAMNULOSE KINASE IN COMPLEX WITH ADP AND BETA-L-RHAMNULOSE.===




==Overview==
<!--
The enzyme L-rhamnulose kinase from Escherichia coli participates in the degradation pathway of L-rhamnose, a common natural deoxy-hexose. The structure of the enzyme in a ternary complex with its substrates ADP and L-rhamnulose has been determined at 1.55A resolution and refined to R(cryst)/R(free) values of 0.179/0.209. The result was compared with the lower resolution structure of a corresponding complex containing L-fructose instead of L-rhamnulose. In light of the two established sugar positions and conformations, a number of rare sugars have been modeled into the active center of L-rhamnulose kinase and the model structures have been compared with the known enzymatic phosphorylation rates. Rare sugars are of rising interest for the synthesis of bioactive compounds.
The line below this paragraph, {{ABSTRACT_PUBMED_17568582}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17568582 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17568582}}


==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures., Grueninger D, Schulz GE, FEBS Lett. 2007 Jun 26;581(16):3127-30. Epub 2007 Jun 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17568582 17568582]
Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures., Grueninger D, Schulz GE, FEBS Lett. 2007 Jun 26;581(16):3127-30. Epub 2007 Jun 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17568582 17568582]
Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli., Grueninger D, Schulz GE, J Mol Biol. 2006 Jun 9;359(3):787-97. Epub 2006 Apr 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16674975 16674975]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Rhamnulokinase]]
[[Category: Rhamnulokinase]]
Line 34: Line 40:
[[Category: Rhamnose metabolism]]
[[Category: Rhamnose metabolism]]
[[Category: Transferase]]
[[Category: Transferase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:49:56 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:26:24 2008''

Revision as of 09:26, 27 July 2008

File:2uyt.png

Template:STRUCTURE 2uyt

STRUCTURE OF L-RHAMNULOSE KINASE IN COMPLEX WITH ADP AND BETA-L-RHAMNULOSE.

Template:ABSTRACT PUBMED 17568582

About this Structure

2UYT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures., Grueninger D, Schulz GE, FEBS Lett. 2007 Jun 26;581(16):3127-30. Epub 2007 Jun 6. PMID:17568582

Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli., Grueninger D, Schulz GE, J Mol Biol. 2006 Jun 9;359(3):787-97. Epub 2006 Apr 25. PMID:16674975

Page seeded by OCA on Sun Jul 27 12:26:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA