1IUG

The crystal structure of aspartate aminotransferase which belongs to subgroup IV from Thermus thermophilus

Summary for 1IUG

• Entry DOI: 10.2210/pdb1iug/pdb
• Descriptor: putative aspartate aminotransferase, PHOSPHATE ION (3 entities in total)
• Functional Keywords: wild type, pyridoxal-5'-phosphate form, riken structural genomics/proteomics initiative, rsgi, structural genomics, transferase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 76718.18

Authors

Katsura, Y.,Shirouzu, M.,Yamaguchi, H.,Ishitani, R.,Nureki, O.,Kuramitsu, S.,Hayashi, H.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-03-04, release date: 2003-11-25, Last modification date: 2024-12-25)

Primary citation

Katsura, Y.,Shirouzu, M.,Yamaguchi, H.,Ishitani, R.,Nureki, O.,Kuramitsu, S.,Hayashi, H.,Yokoyama, S.
Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV.
Proteins, 55:487-492, 2004

PubMed Abstract: 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.

PubMed: 15103612
DOI: 10.1002/prot.20020

Experimental method

X-RAY DIFFRACTION (2.2 Å)