1iug
From Proteopedia
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|PDB= 1iug |SIZE=350|CAPTION= <scene name='initialview01'>1iug</scene>, resolution 2.2Å | |PDB= 1iug |SIZE=350|CAPTION= <scene name='initialview01'>1iug</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | + | |LIGAND= <scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iug OCA], [http://www.ebi.ac.uk/pdbsum/1iug PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iug RCSB]</span> | ||
}} | }} | ||
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[[Category: Yamaguchi, H.]] | [[Category: Yamaguchi, H.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: PO4]] | ||
[[Category: pyridoxal-5'-phosphate form]] | [[Category: pyridoxal-5'-phosphate form]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
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[[Category: wild type]] | [[Category: wild type]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:24:52 2008'' |
Revision as of 18:24, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus
Overview
Protein TT0402 from Thermus thermophilus HB8 exhibits about 30-35% sequence identity with proteins belonging to subgroup IV in the aminotransferase family of the fold-type I pyridoxal 5'-phosphate (PLP)-dependent enzymes. In this study, we determined the crystal structure of TT0402 at 2.3 A resolution (R(factor) = 19.9%, R(free) = 23.6%). The overall structure of TT0402 exhibits the fold conserved in aminotransferases, and is most similar to that of the Escherichia coli phosphoserine aminotransferase, which belongs to subgroup IV but shares as little as 13% sequence identity with TT0402. Kinetic assays confirmed that TT0402 has higher transamination activities with the amino group donor, L-glutamate, and somewhat lower activities with L-aspartate. These results indicate that TT0402 is a subgroup IV aminotransferase for the synthesis/degradation of either L-aspartate or a similar compound.
About this Structure
1IUG is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV., Katsura Y, Shirouzu M, Yamaguchi H, Ishitani R, Nureki O, Kuramitsu S, Hayashi H, Yokoyama S, Proteins. 2004 May 15;55(3):487-92. PMID:15103612
Page seeded by OCA on Sun Mar 30 21:24:52 2008
Categories: Single protein | Thermus thermophilus | Hayashi, H. | Ishitani, R. | Katsura, Y. | Kuramitsu, S. | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shirouzu, M. | Yamaguchi, H. | Yokoyama, S. | Pyridoxal-5'-phosphate form | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | Wild type
