1f0k

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(New page: 200px<br /><applet load="1f0k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f0k, resolution 1.9&Aring;" /> '''THE 1.9 ANGSTROM CRYS...)
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'''THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG'''<br />
'''THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG'''<br />
==Overview==
==Overview==
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The 1.9 A X-ray structure of a membrane-associated glycosyltransferase, involved in peptidoglycan biosynthesis is reported. This enzyme, MurG, contains two alpha/beta open sheet domains separated by a deep cleft., Structural analysis suggests that the C-terminal domain contains the, UDP-GlcNAc binding site while the N-terminal domain contains the acceptor, binding site and likely membrane association site. Combined with sequence, data from other MurG homologs, this structure provides insight into the, residues that are important in substrate binding and catalysis. We have, also noted that a conserved region found in many UDP-sugar transferases, maps to a beta/alpha/beta/alpha supersecondary structural motif in the, donor binding region of MurG, an observation that may be helpful in, glycosyltransferase structure prediction. The identification of a, conserved structural motif involved in donor binding in different, UDP-sugar transferases also suggests that it may be possible to, identify--and perhaps alter--the residues that help determine donor, specificity.
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The 1.9 A X-ray structure of a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis is reported. This enzyme, MurG, contains two alpha/beta open sheet domains separated by a deep cleft. Structural analysis suggests that the C-terminal domain contains the UDP-GlcNAc binding site while the N-terminal domain contains the acceptor binding site and likely membrane association site. Combined with sequence data from other MurG homologs, this structure provides insight into the residues that are important in substrate binding and catalysis. We have also noted that a conserved region found in many UDP-sugar transferases maps to a beta/alpha/beta/alpha supersecondary structural motif in the donor binding region of MurG, an observation that may be helpful in glycosyltransferase structure prediction. The identification of a conserved structural motif involved in donor binding in different UDP-sugar transferases also suggests that it may be possible to identify--and perhaps alter--the residues that help determine donor specificity.
==About this Structure==
==About this Structure==
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1F0K 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F0K OCA].
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1F0K 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0K OCA].
==Reference==
==Reference==
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[[Category: rossmann fold]]
[[Category: rossmann fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:30:09 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:29 2008''

Revision as of 10:33, 21 February 2008

Image:1f0k.gif

1f0k, resolution 1.9Å

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THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG

Overview

The 1.9 A X-ray structure of a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis is reported. This enzyme, MurG, contains two alpha/beta open sheet domains separated by a deep cleft. Structural analysis suggests that the C-terminal domain contains the UDP-GlcNAc binding site while the N-terminal domain contains the acceptor binding site and likely membrane association site. Combined with sequence data from other MurG homologs, this structure provides insight into the residues that are important in substrate binding and catalysis. We have also noted that a conserved region found in many UDP-sugar transferases maps to a beta/alpha/beta/alpha supersecondary structural motif in the donor binding region of MurG, an observation that may be helpful in glycosyltransferase structure prediction. The identification of a conserved structural motif involved in donor binding in different UDP-sugar transferases also suggests that it may be possible to identify--and perhaps alter--the residues that help determine donor specificity.

About this Structure

1F0K is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

The 1.9 A crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis., Ha S, Walker D, Shi Y, Walker S, Protein Sci. 2000 Jun;9(6):1045-52. PMID:10892798

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