2icy: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2icy.gif|left|200px]]
{{Seed}}
[[Image:2icy.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2icy|  PDB=2icy  |  SCENE=  }}  
{{STRUCTURE_2icy|  PDB=2icy  |  SCENE=  }}  


'''Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UDP-glucose'''
===Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UDP-glucose===




==Overview==
<!--
The structure of the UDP-glucose pyrophosphorylase encoded by Arabidopsis thaliana gene At3g03250 has been solved to a nominal resolution of 1.86 Angstroms. In addition, the structure has been solved in the presence of the substrates/products UTP and UDP-glucose to nominal resolutions of 1.64 Angstroms and 1.85 Angstroms. The three structures revealed a catalytic domain similar to that of other nucleotidyl-glucose pyrophosphorylases with a carboxy-terminal beta-helix domain in a unique orientation. Conformational changes are observed between the native and substrate-bound complexes. The nucleotide-binding loop and the carboxy-terminal domain, including the suspected catalytically important Lys360, move in and out of the active site in a concerted fashion. TLS refinement was employed initially to model conformational heterogeneity in the UDP-glucose complex followed by the use of multiconformer refinement for the entire molecule. Normal mode analysis generated atomic displacement predictions in good agreement in magnitude and direction with the observed conformational changes and anisotropic displacement parameters generated by TLS refinement. The structures and the observed dynamic changes provide insight into the ordered mechanism of this enzyme and previously described oligomerization effects on catalytic activity.
The line below this paragraph, {{ABSTRACT_PUBMED_17178129}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17178129 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17178129}}


==About this Structure==
==About this Structure==
Line 38: Line 42:
[[Category: Structural genomics functional follow-up study]]
[[Category: Structural genomics functional follow-up study]]
[[Category: Udp]]
[[Category: Udp]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:20:56 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:32:59 2008''

Revision as of 09:32, 10 July 2008

File:2icy.png

Template:STRUCTURE 2icy

Crystal Structure of a Putative UDP-glucose Pyrophosphorylase from Arabidopsis Thaliana with Bound UDP-glucose

Template:ABSTRACT PUBMED 17178129

About this Structure

2ICY is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP., McCoy JG, Bitto E, Bingman CA, Wesenberg GE, Bannen RM, Kondrashov DA, Phillips GN Jr, J Mol Biol. 2007 Feb 23;366(3):830-41. Epub 2006 Nov 21. PMID:17178129

Page seeded by OCA on Thu Jul 10 12:32:59 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2icy&oldid=638306"