1bhn: Difference between revisions

Revision as of 19:10, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1bhn.png

Template:STRUCTURE 1bhn

NUCLEOSIDE DIPHOSPHATE KINASE ISOFORM A FROM BOVINE RETINANUCLEOSIDE DIPHOSPHATE KINASE ISOFORM A FROM BOVINE RETINA

Template:ABSTRACT PUBMED 10329774

About this StructureAbout this Structure

1BHN is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

The three-dimensional structures of two isoforms of nucleoside diphosphate kinase from bovine retina., Ladner JE, Abdulaev NG, Kakuev DL, Tordova M, Ridge KD, Gilliland GL, Acta Crystallogr D Biol Crystallogr. 1999 Jun;55(Pt 6):1127-35. PMID:10329774

Page seeded by OCA on Mon Jun 30 19:10:56 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1bhn.gif|left|200px]]
+{{Seed}}
+[[Image:1bhn.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1bhn|  PDB=1bhn  |  SCENE=  }}
-'''NUCLEOSIDE DIPHOSPHATE KINASE ISOFORM A FROM BOVINE RETINA'''
+===NUCLEOSIDE DIPHOSPHATE KINASE ISOFORM A FROM BOVINE RETINA===
-==Overview==
+<!--
-The crystal structures of two isoforms of nucleoside diphosphate kinase from bovine retina overexpressed in Escherischia coli have been determined to 2.4 A resolution. Both the isoforms, NBR-A and NBR-B, are hexameric and the fold of the monomer is in agreement with NDP-kinase structures from other biological sources. Although the polypeptide chains of the two isoforms differ by only two residues, they crystallize in different space groups. NBR-A crystallizes in space group P212121 with an entire hexamer in the asymmetric unit, while NBR-B crystallizes in space group P43212 with a trimer in the asymmetric unit. The highly conserved nucleotide-binding site observed in other nucleoside diphosphate kinase structures is also observed here. Both NBR-A and NBR-B were crystallized in the presence of cGMP. The nucleotide is bound with the base in the anti conformation. The NBR-A active site contained both cGMP and GDP each bound at half occupancy. Presumably, NBR-A had retained GDP (or GTP) from the purification process. The NBR-B active site contained only cGMP.
+The line below this paragraph, {{ABSTRACT_PUBMED_10329774}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10329774 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10329774}}
 ==About this Structure==
@@ Line 33: / Line 37: @@
 [[Category: Tordova, M.]]
 [[Category: Phosphotransferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:31:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:10:56 2008''