1l2u: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1l2u.jpg|left|200px]]
{{Seed}}
[[Image:1l2u.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1l2u|  PDB=1l2u  |  SCENE=  }}  
{{STRUCTURE_1l2u|  PDB=1l2u  |  SCENE=  }}  


'''Orotidine 5'-monophosphate decarboxylase from E. coli'''
===Orotidine 5'-monophosphate decarboxylase from E. coli===




==Overview==
<!--
Orotidine 5'-monophosphate decarboxylase (ODCase) catalyses the decarboxylation of orotidine 5'-monophosphate to uridine 5'-monophosphate (UMP). We have earlier determined the structure of ODCase from Escherichia coli complexed with the inhibitor 1-(5'-phospho-beta-d-ribofuranosyl)barbituric acid (BMP); here we present the 2.5 A structure of the uncomplexed apo enzyme, determined from twinned crystals. A structural analysis and comparison of the two structures of the E. coli enzyme show that binding of the inhibitor is accompanied by significant domain movements of approximately 12 degrees around a hinge that crosses the active site. Hence, the ODCase dimer, which contains two active sites, may be divided in three domains: a central domain that is fixed, and two lids which independently move 12 degrees upon binding. Corresponding analyses, presented herein, of the two Saccharomyces cerevisiae ODCase structures (with and without BMP) and the Methanobacterium thermoautotrophicum ODCase structures (with and without 6-aza UMP) show very similar, but somewhat smaller domain movements. The domain movements seem to be initiated by the phosphoryl binding to the enzyme and can explain why the binding of the phosphoryl group is essential for the catalytic function.
The line below this paragraph, {{ABSTRACT_PUBMED_12054799}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12054799 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12054799}}


==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Twinned crystal]]
[[Category: Twinned crystal]]
[[Category: X-ray diffraction]]
[[Category: X-ray diffraction]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:28:46 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:34:49 2008''

Revision as of 08:34, 2 July 2008

File:1l2u.png

Template:STRUCTURE 1l2u

Orotidine 5'-monophosphate decarboxylase from E. coli

Template:ABSTRACT PUBMED 12054799

About this Structure

1L2U is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase., Harris P, Poulsen JC, Jensen KF, Larsen S, J Mol Biol. 2002 May 10;318(4):1019-29. PMID:12054799

Page seeded by OCA on Wed Jul 2 11:34:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1l2u&oldid=623676"