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[[Image:1f0k.gif|left|200px]]<br /><applet load="1f0k" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f0k, resolution 1.9&Aring;" />
'''THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG'''<br />


==Overview==
==THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG==
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.
<StructureSection load='1f0k' size='340' side='right'caption='[[1f0k]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f0k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F0K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F0K FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f0k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f0k OCA], [https://pdbe.org/1f0k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f0k RCSB], [https://www.ebi.ac.uk/pdbsum/1f0k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f0k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MURG_ECOLI MURG_ECOLI] Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).[HAMAP-Rule:MF_00033]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f0/1f0k_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f0k ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[O-GlcNAc transferase 3D structures|O-GlcNAc transferase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10892798 10892798]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ha, S.]]
[[Category: Ha S]]
[[Category: Shi, Y.]]
[[Category: Shi Y]]
[[Category: Walker, D.]]
[[Category: Walker D]]
[[Category: Walker, S.]]
[[Category: Walker S]]
[[Category: SO4]]
[[Category: rossmann fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:29 2008''

Latest revision as of 10:09, 7 February 2024

THE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURGTHE 1.9 ANGSTROM CRYSTAL STRUCTURE OF E. COLI MURG

Structural highlights

1f0k is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MURG_ECOLI Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).[HAMAP-Rule:MF_00033]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1f0k, resolution 1.90Å

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