1jsw

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[[Image:1jsw.gif|left|200px]]
[[Image:1jsw.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1jsw |SIZE=350|CAPTION= <scene name='initialview01'>1jsw</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1jsw", 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</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_ammonia-lyase Aspartate ammonia-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.1.1 4.3.1.1] </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_1jsw| PDB=1jsw | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jsw OCA], [http://www.ebi.ac.uk/pdbsum/1jsw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jsw RCSB]</span>
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}}
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'''NATIVE L-ASPARTATE AMMONIA LYASE'''
'''NATIVE L-ASPARTATE AMMONIA LYASE'''
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[[Category: Farber, G K.]]
[[Category: Farber, G K.]]
[[Category: Shi, W.]]
[[Category: Shi, W.]]
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[[Category: amino acid ammonia-lyase]]
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[[Category: Amino acid ammonia-lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:52:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:38:30 2008''
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Revision as of 18:52, 2 May 2008

Image:1jsw.gif

Template:STRUCTURE 1jsw

NATIVE L-ASPARTATE AMMONIA LYASE


Overview

The X-ray crystal structure of l-aspartate ammonia-lyase has been determined to 2.8 A resolution. The enzyme contains three domains, and each domain is composed almost completely of alpha helices. The central domain is composed of five long helices. In the tetramer, these five helices form a 20-helix cluster. Such clusters have also been seen in delta-crystallin and in fumarase. The active site of aspartase has been located in a region that contains side chains from three different subunits. The structure of the apoenzyme has made it possible to identify some of the residues that are involved in binding the substrate. These residues have been examined by site-directed mutagenesis, and their putative roles have been assigned [Jayasekera, M. M. K., Shi, W., Farber, G. K., & Viola, R. E. (1997) Biochemistry 36, 9145-9150].

About this Structure

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

Reference

The structure of L-aspartate ammonia-lyase from Escherichia coli., Shi W, Dunbar J, Jayasekera MM, Viola RE, Farber GK, Biochemistry. 1997 Jul 29;36(30):9136-44. PMID:9230045 Page seeded by OCA on Fri May 2 21:52:00 2008

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