1jsw

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(New page: 200px<br /><applet load="1jsw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jsw, resolution 2.7&Aring;" /> '''NATIVE L-ASPARTATE AM...)
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'''NATIVE L-ASPARTATE AMMONIA LYASE'''<br />
'''NATIVE L-ASPARTATE AMMONIA LYASE'''<br />
==Overview==
==Overview==
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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., &amp; Viola, R. E. (1997) Biochemistry 36, 9145-9150].
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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., &amp; Viola, R. E. (1997) Biochemistry 36, 9145-9150].
==About this Structure==
==About this Structure==
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1JSW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GLC and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JSW OCA].
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1JSW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=GLC:'>GLC</scene> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JSW OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Dunbar, J.]]
[[Category: Dunbar, J.]]
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[[Category: Farber, G.K.]]
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[[Category: Farber, G K.]]
[[Category: Shi, W.]]
[[Category: Shi, W.]]
[[Category: ACT]]
[[Category: ACT]]
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[[Category: amino acid ammonia-lyase]]
[[Category: amino acid ammonia-lyase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:32:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:26 2008''

Revision as of 11:26, 21 February 2008


1jsw, resolution 2.7Å

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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 with and as ligands. Active as Aspartate ammonia-lyase, with EC number 4.3.1.1 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

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