1la2

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(New page: 200px<br /><applet load="1la2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1la2, resolution 2.65&Aring;" /> '''Structural analysis ...)
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[[Image:1la2.gif|left|200px]]<br /><applet load="1la2" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1la2.gif|left|200px]]<br /><applet load="1la2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1la2, resolution 2.65&Aring;" />
caption="1la2, resolution 2.65&Aring;" />
'''Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase'''<br />
'''Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase'''<br />
==Overview==
==Overview==
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The New York Structural Genomics Research Consortium has targeted highly, conserved but uncharacterized enzyme families for structure determination., As part of this effort, the 2.65-A crystal structure has been determined, for Saccharomyces cerevisiae myo-inositol 1-phosphate synthase (MIP), an, essential enzyme that catalyzes critical steps in inositol biosynthesis., The structure determination of four independent monomers in the asymmetric, unit (240 kDa) reveals atomic details and residue composition for the, partially closed NAD-containing active sites in apo-configuration. The, structure further reveals extensive interactions involved in tetrameric, assembly of the enzyme complex.
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The New York Structural Genomics Research Consortium has targeted highly conserved but uncharacterized enzyme families for structure determination. As part of this effort, the 2.65-A crystal structure has been determined for Saccharomyces cerevisiae myo-inositol 1-phosphate synthase (MIP), an essential enzyme that catalyzes critical steps in inositol biosynthesis. The structure determination of four independent monomers in the asymmetric unit (240 kDa) reveals atomic details and residue composition for the partially closed NAD-containing active sites in apo-configuration. The structure further reveals extensive interactions involved in tetrameric assembly of the enzyme complex.
==About this Structure==
==About this Structure==
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1LA2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inositol-3-phosphate_synthase Inositol-3-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.4 5.5.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LA2 OCA].
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1LA2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inositol-3-phosphate_synthase Inositol-3-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.5.1.4 5.5.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LA2 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Beckwith, A.]]
[[Category: Beckwith, A.]]
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[[Category: Buglino, J.A.]]
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[[Category: Buglino, J A.]]
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[[Category: Burley, S.K.]]
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[[Category: Burley, S K.]]
[[Category: Chadna, T.]]
[[Category: Chadna, T.]]
[[Category: Kniewel, R.]]
[[Category: Kniewel, R.]]
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[[Category: Lima, C.D.]]
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[[Category: Lima, C D.]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
[[Category: Shen, V.]]
[[Category: Shen, V.]]
[[Category: NAD]]
[[Category: NAD]]
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[[Category: yeast]]
[[Category: yeast]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:25:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:58 2008''

Revision as of 11:43, 21 February 2008


1la2, resolution 2.65Å

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Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase

Overview

The New York Structural Genomics Research Consortium has targeted highly conserved but uncharacterized enzyme families for structure determination. As part of this effort, the 2.65-A crystal structure has been determined for Saccharomyces cerevisiae myo-inositol 1-phosphate synthase (MIP), an essential enzyme that catalyzes critical steps in inositol biosynthesis. The structure determination of four independent monomers in the asymmetric unit (240 kDa) reveals atomic details and residue composition for the partially closed NAD-containing active sites in apo-configuration. The structure further reveals extensive interactions involved in tetrameric assembly of the enzyme complex.

About this Structure

1LA2 is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. Active as Inositol-3-phosphate synthase, with EC number 5.5.1.4 Full crystallographic information is available from OCA.

Reference

Structural analysis of Saccharomyces cerevisiae myo-inositol phosphate synthase., Kniewel R, Buglino JA, Shen V, Chadha T, Beckwith A, Lima CD, J Struct Funct Genomics. 2002;2(3):129-34. PMID:12836703

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