1uu0: Difference between revisions
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'''HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)''' | {{Structure | ||
|PDB= 1uu0 |SIZE=350|CAPTION= <scene name='initialview01'>1uu0</scene>, resolution 2.85Å | |||
|SITE= <scene name='pdbsite=AC1:Po4+Binding+Site+For+Chain+D'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Histidinol-phosphate_transaminase Histidinol-phosphate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.9 2.6.1.9] | |||
|GENE= | |||
}} | |||
'''HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1UU0 is a [ | 1UU0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UU0 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15007066 15007066] | ||
[[Category: Histidinol-phosphate transaminase]] | [[Category: Histidinol-phosphate transaminase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:36:44 2008'' | ||
Revision as of 15:36, 20 March 2008
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| , resolution 2.85Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Histidinol-phosphate transaminase, with EC number 2.6.1.9 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HISTIDINOL-PHOSPHATE AMINOTRANSFERASE (HISC) FROM THERMOTOGA MARITIMA (APO-FORM)
OverviewOverview
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.
About this StructureAbout this Structure
1UU0 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
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