1czc

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[[Image:1czc.jpg|left|200px]]
[[Image:1czc.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1czc |SIZE=350|CAPTION= <scene name='initialview01'>1czc</scene>, resolution 2.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1czc", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GUA:GLUTARIC+ACID'>GUA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1czc| PDB=1czc | SCENE= }}
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|RELATEDENTRY=[[1yoo|1YOO]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1czc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1czc OCA], [http://www.ebi.ac.uk/pdbsum/1czc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1czc RCSB]</span>
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}}
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'''ASPARTATE AMINOTRANSFERASE MUTANT ATB17/139S/142N WITH GLUTARIC ACID'''
'''ASPARTATE AMINOTRANSFERASE MUTANT ATB17/139S/142N WITH GLUTARIC ACID'''
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[[Category: Oue, S.]]
[[Category: Oue, S.]]
[[Category: Yano, T.]]
[[Category: Yano, T.]]
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[[Category: aspartate aminotransferase]]
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[[Category: Aspartate aminotransferase]]
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[[Category: substrate specificity]]
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[[Category: Substrate specificity]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:16:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:31:24 2008''
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Revision as of 10:16, 2 May 2008

Image:1czc.jpg

Template:STRUCTURE 1czc

ASPARTATE AMINOTRANSFERASE MUTANT ATB17/139S/142N WITH GLUTARIC ACID


Overview

A mutant Escherichia coil aspartate aminotransferase with 17 amino acid substitutions (ATB17), previously created by directed evolution, shows increased activity for beta-branched amino acids and decreased activity for the native substrates, aspartate and glutamate. A new mutant (ATBSN) was generated by changing two of the 17 mutated residues back to the original ones. ATBSN recovered the activities for aspartate and glutamate to the level of the wild-type enzyme while maintaining the enhanced activity of ATB17 for the other amino acid substrates. The absorption spectrum of the bound coenzyme, pyridoxal 5'-phosphate, also returned to the original state. ATBSN shows significantly increased affinity for substrate analogs including succinate and glutarate, analogs of aspartate and glutamate, respectively. Hence, we could cocrystallize ATBSN with succinate or glutarate, and the structures show how the enzyme can bind two kinds of dicarboxylic substrates with different chain lengths. The present results may also provide an insight into the long-standing controversies regarding the mode of binding of glutamate to the wild-type enzyme.

About this Structure

1CZC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex., Oue S, Okamoto A, Yano T, Kagamiyama H, J Biochem. 2000 Feb;127(2):337-43. PMID:10731702 Page seeded by OCA on Fri May 2 13:16:15 2008

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