1gc3
From Proteopedia
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| - | [[Image:1gc3.jpg|left|200px]] | + | [[Image:1gc3.jpg|left|200px]] |
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| - | '''THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 COMPLEXED WITH TRYPTOPHAN''' | + | {{Structure |
| + | |PDB= 1gc3 |SIZE=350|CAPTION= <scene name='initialview01'>1gc3</scene>, resolution 3.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 COMPLEXED WITH TRYPTOPHAN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GC3 is a [ | + | 1GC3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GC3 OCA]. |
==Reference== | ==Reference== | ||
| - | Substrate recognition mechanism of thermophilic dual-substrate enzyme., Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S, J Biochem. 2001 Jul;130(1):89-98. PMID:[http:// | + | Substrate recognition mechanism of thermophilic dual-substrate enzyme., Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S, J Biochem. 2001 Jul;130(1):89-98. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11432784 11432784] |
[[Category: Aspartate transaminase]] | [[Category: Aspartate transaminase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: pyridoxal enzyme]] | [[Category: pyridoxal enzyme]] | ||
| - | ''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 11:21:08 2008'' |
Revision as of 09:21, 20 March 2008
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| , resolution 3.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aspartate transaminase, with EC number 2.6.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THERMUS THERMOPHILUS ASPARTATE AMINOTRANSFERASE TETRA MUTANT 2 COMPLEXED WITH TRYPTOPHAN
Overview
Aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (ttAspAT), has been believed to be specific for an acidic substrate. However, stepwise introduction of mutations in the active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme. The final mutant, [S15D, T17V, K109S, S292R] ttAspAT, is active toward both acidic and hydrophobic substrates. During the course of stepwise mutation, the activities toward acidic and hydrophobic substrates changed independently. The introduction of a mobile Arg292* residue into ttAspAT was the key step in the change to a "dual-substrate" enzyme. The substrate recognition mechanism of this thermostable "dual-substrate" enzyme was confirmed by X-ray crystallography. This work together with previous studies on various enzymes suggest that this unique "dual-substrate recognition" mechanism is a feature of not only aminotransferases but also other enzymes.
About this Structure
1GC3 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Substrate recognition mechanism of thermophilic dual-substrate enzyme., Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S, J Biochem. 2001 Jul;130(1):89-98. PMID:11432784
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