1cke: 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:1cke.gif|left|200px]]
{{Seed}}
[[Image:1cke.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1cke|  PDB=1cke  |  SCENE=  }}  
{{STRUCTURE_1cke|  PDB=1cke  |  SCENE=  }}  


'''CMP KINASE FROM ESCHERICHIA COLI FREE ENZYME STRUCTURE'''
===CMP KINASE FROM ESCHERICHIA COLI FREE ENZYME STRUCTURE===




==Overview==
<!--
Background:. Nucleoside monophosphate kinases (NMP kinases) catalyze the reversible transfer of a phosphoryl group from a nucleoside triphosphate to a nucleoside monophosphate. Among them, cytidine monophosphate kinase from Escherichia coli has a striking particularity: it is specific for CMP, whereas in eukaryotes a unique UMP/CMP kinase phosphorylates both CMP and UMP with similar efficiency. Results:. The crystal structure of the CMP kinase apoenzyme from E. coli was solved by single isomorphous replacement and refined at 1.75 A resolution. The structure of the enzyme in complex with CDP was determined at 2.0 A resolution. Like other NMP kinases, the protein contains a central parallel beta sheet, the strands of which are connected by alpha helices. The enzyme differs from other NMP kinases in the presence of a 40-residue insert situated in the NMP-binding (NMPbind) domain. This insert contains two domains: one comprising a three-stranded antiparallel beta sheet, the other comprising two alpha helices. Conclusions:. Two features of the CMP kinase from E. coli have no equivalent in other NMP kinases of known structure. Firstly, the large NMPbind insert undergoes a CDP-induced rearrangement: its beta-sheet domain moves away from the substrate, whereas its helical domain comes closer to it in a motion likely to improve the protection of the active site. Secondly, residues involved in CDP recognition are conserved in CMP kinases and have no counterpart in other NMP kinases. The structures presented here are the first of a new family of NMP kinases specific for CMP.
The line below this paragraph, {{ABSTRACT_PUBMED_9862805}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9862805 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9862805}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Golinelli-Pimpaneau, B.]]
[[Category: Golinelli-Pimpaneau, B.]]
[[Category: Nucleotide monophosphate kinase]]
[[Category: Nucleotide monophosphate kinase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:49:41 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:52:05 2008''

Revision as of 17:52, 30 June 2008

File:1cke.png

Template:STRUCTURE 1cke

CMP KINASE FROM ESCHERICHIA COLI FREE ENZYME STRUCTURE

Template:ABSTRACT PUBMED 9862805

About this Structure

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

Reference

Structures of escherichia coli CMP kinase alone and in complex with CDP: a new fold of the nucleoside monophosphate binding domain and insights into cytosine nucleotide specificity., Briozzo P, Golinelli-Pimpaneau B, Gilles AM, Gaucher JF, Burlacu-Miron S, Sakamoto H, Janin J, Barzu O, Structure. 1998 Dec 15;6(12):1517-27. PMID:9862805

Page seeded by OCA on Mon Jun 30 20:52:05 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1cke&oldid=583033"