1m5w

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(New page: 200px<br /><applet load="1m5w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5w, resolution 1.96&Aring;" /> '''1.96 A Crystal Struc...)
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[[Image:1m5w.gif|left|200px]]<br /><applet load="1m5w" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1m5w.gif|left|200px]]<br /><applet load="1m5w" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m5w, resolution 1.96&Aring;" />
caption="1m5w, resolution 1.96&Aring;" />
'''1.96 A Crystal Structure of Pyridoxine 5'-Phosphate Synthase in Complex with 1-deoxy-D-xylulose phosphate'''<br />
'''1.96 A Crystal Structure of Pyridoxine 5'-Phosphate Synthase in Complex with 1-deoxy-D-xylulose phosphate'''<br />
==Overview==
==Overview==
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We report the 1.96 A crystal structure of pyridoxine 5'-phosphate synthase, (PdxJ) in complex with 1-deoxy-D-xylulose phosphate (dXP). The octameric, enzyme possesses eight distinct binding sites, and three different binding, states are observed. The observation of these three states supports a, mechanism in which precise conformational changes of a peptide loop and, groups of active site residues modulate binding and specificity. The, differences in protein conformation when one or two substrates are bound, can be correlated with a condensation mechanism that leads productively to, the formation of pyridoxine 5'-phosphate (PNP). "Snapshots" of the, progression from the apo form to a singly occupied "transitional binding", state and, subsequently, to a fully occupied, reactive state are revealed, and indicate how the enzyme structure can be related to a plausible, catalytic mechanism and, moreover, to favorable energetics of reaction.
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We report the 1.96 A crystal structure of pyridoxine 5'-phosphate synthase (PdxJ) in complex with 1-deoxy-D-xylulose phosphate (dXP). The octameric enzyme possesses eight distinct binding sites, and three different binding states are observed. The observation of these three states supports a mechanism in which precise conformational changes of a peptide loop and groups of active site residues modulate binding and specificity. The differences in protein conformation when one or two substrates are bound can be correlated with a condensation mechanism that leads productively to the formation of pyridoxine 5'-phosphate (PNP). "Snapshots" of the progression from the apo form to a singly occupied "transitional binding" state and, subsequently, to a fully occupied, reactive state are revealed and indicate how the enzyme structure can be related to a plausible catalytic mechanism and, moreover, to favorable energetics of reaction.
==About this Structure==
==About this Structure==
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1M5W 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 DXP and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M5W OCA].
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1M5W 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=DXP:'>DXP</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5W OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Cane, D.E.]]
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[[Category: Cane, D E.]]
[[Category: Du, S.]]
[[Category: Du, S.]]
[[Category: Pohl, E.]]
[[Category: Pohl, E.]]
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[[Category: Yeh, J.I.]]
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[[Category: Yeh, J I.]]
[[Category: DXP]]
[[Category: DXP]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: tim barrel]]
[[Category: tim barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:10:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:48 2008''

Revision as of 11:51, 21 February 2008


1m5w, resolution 1.96Å

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1.96 A Crystal Structure of Pyridoxine 5'-Phosphate Synthase in Complex with 1-deoxy-D-xylulose phosphate

Overview

We report the 1.96 A crystal structure of pyridoxine 5'-phosphate synthase (PdxJ) in complex with 1-deoxy-D-xylulose phosphate (dXP). The octameric enzyme possesses eight distinct binding sites, and three different binding states are observed. The observation of these three states supports a mechanism in which precise conformational changes of a peptide loop and groups of active site residues modulate binding and specificity. The differences in protein conformation when one or two substrates are bound can be correlated with a condensation mechanism that leads productively to the formation of pyridoxine 5'-phosphate (PNP). "Snapshots" of the progression from the apo form to a singly occupied "transitional binding" state and, subsequently, to a fully occupied, reactive state are revealed and indicate how the enzyme structure can be related to a plausible catalytic mechanism and, moreover, to favorable energetics of reaction.

About this Structure

1M5W is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.

Reference

Multistate binding in pyridoxine 5'-phosphate synthase: 1.96 A crystal structure in complex with 1-deoxy-D-xylulose phosphate., Yeh JI, Du S, Pohl E, Cane DE, Biochemistry. 2002 Oct 1;41(39):11649-57. PMID:12269807

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