1uu1: Difference between revisions

Revision as of 10:55, 29 July 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:1uu1.png

Template:STRUCTURE 1uu1

COMPLEX OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)COMPLEX OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)

Template:ABSTRACT PUBMED 15007066

About this StructureAbout this Structure

1UU1 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

ReferenceReference

Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase., Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M, J Biol Chem. 2004 May 14;279(20):21478-88. Epub 2004 Mar 8. PMID:15007066

Page seeded by OCA on Tue Jul 29 10:55:21 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1uu1.jpg|left|200px]]
+{{Seed}}
+[[Image:1uu1.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1uu1|  PDB=1uu1  |  SCENE=  }}
-'''COMPLEX OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)'''
+===COMPLEX OF HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)===
-==Overview==
+<!--
-In histidine biosynthesis, histidinol-phosphate aminotransferase catalyzes the transfer of the amino group from glutamate to imidazole acetol-phosphate producing 2-oxoglutarate and histidinol phosphate. In some organisms such as the hyperthermophile Thermotoga maritima, specific tyrosine and aromatic amino acid transaminases have not been identified to date, suggesting an additional role for histidinol-phosphate aminotransferase in other transamination reactions generating aromatic amino acids. To gain insight into the specific function of this transaminase, we have determined its crystal structure in the absence of any ligand except phosphate, in the presence of covalently bound pyridoxal 5'-phosphate, of the coenzyme histidinol phosphate adduct, and of pyridoxamine 5'-phosphate. The enzyme accepts histidinol phosphate, tyrosine, tryptophan, and phenylalanine, but not histidine, as substrates. The structures provide a model of how these different substrates could be accommodated by histidinol-phosphate aminotransferase. Some of the structural features of the enzyme are more preserved between the T. maritima enzyme and a related threonine-phosphate decarboxylase from S. typhimurium than with histidinol-phosphate aminotransferases from different organisms.
+The line below this paragraph, {{ABSTRACT_PUBMED_15007066}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15007066 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15007066}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Pyridoxal phosphate]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:41:20 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:55:21 2008''