1tj7

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(New page: 200px<br /><applet load="1tj7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tj7, resolution 2.44&Aring;" /> '''Structure determinat...)
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[[Image:1tj7.gif|left|200px]]<br /><applet load="1tj7" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1tj7.gif|left|200px]]<br /><applet load="1tj7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tj7, resolution 2.44&Aring;" />
caption="1tj7, resolution 2.44&Aring;" />
'''Structure determination and refinement at 2.44 A resolution of Argininosuccinate lyase from E. coli'''<br />
'''Structure determination and refinement at 2.44 A resolution of Argininosuccinate lyase from E. coli'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1TJ7 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 PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TJ7 OCA].
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1TJ7 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=PO4:'>PO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJ7 OCA].
==Reference==
==Reference==
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[[Category: Bergman, U.]]
[[Category: Bergman, U.]]
[[Category: Bhaumik, P.]]
[[Category: Bhaumik, P.]]
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[[Category: Koski, M.K.]]
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[[Category: Koski, M K.]]
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[[Category: Wierenga, R.K.]]
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[[Category: Wierenga, R K.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: fumarase]]
[[Category: fumarase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:07 2008''

Revision as of 13:14, 21 February 2008


1tj7, resolution 2.44Å

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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 with and as ligands. Active as Argininosuccinate lyase, with EC number 4.3.2.1 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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