1tj7

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|PDB= 1tj7 |SIZE=350|CAPTION= <scene name='initialview01'>1tj7</scene>, resolution 2.44&Aring;
|PDB= 1tj7 |SIZE=350|CAPTION= <scene name='initialview01'>1tj7</scene>, resolution 2.44&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tj7 OCA], [http://www.ebi.ac.uk/pdbsum/1tj7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tj7 RCSB]</span>
}}
}}
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[[Category: Koski, M K.]]
[[Category: Koski, M K.]]
[[Category: Wierenga, R K.]]
[[Category: Wierenga, R K.]]
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[[Category: GOL]]
 
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[[Category: PO4]]
 
[[Category: argininosuccinate lyase]]
[[Category: argininosuccinate lyase]]
[[Category: aspartase]]
[[Category: aspartase]]
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[[Category: fumarase]]
[[Category: fumarase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:56:46 2008''

Revision as of 20:56, 30 March 2008


PDB ID 1tj7

Drag the structure with the mouse to rotate
, resolution 2.44Å
Ligands: ,
Activity: Argininosuccinate lyase, with EC number 4.3.2.1
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Structure determination and refinement at 2.44 A resolution of Argininosuccinate lyase from E. coli


Overview

Escherichia coli argininosuccinate lyase has been crystallized from a highly concentrated sample of purified recombinant alpha-methylacyl-CoA racemase, in which it occurred as a minor impurity. The structure has been solved using molecular replacement at 2.44 A resolution. The enzyme is tetrameric, but in this crystal form there is a dimer in the asymmetric unit. The tetramer has four active sites; each active site is constructed from loops of three different subunits. One of these catalytic loops, near residues Ser277 and Ser278, was disordered in previous structures of active lyases, but is very well ordered in this structure in one of the subunits owing to the presence of two phosphate ions in the active-site cavity. The positions of these phosphate ions indicate a plausible mode of binding of the succinate moiety of the substrate in the competent catalytic complex.

About this Structure

1TJ7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli., Bhaumik P, Koski MK, Bergmann U, Wierenga RK, Acta Crystallogr D Biol Crystallogr. 2004 Nov;60(Pt 11):1964-70. Epub 2004, Oct 20. PMID:15502303

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