1uxy: Difference between revisions

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[[Image:1uxy.jpg|left|200px]]


{{Structure
==MURB MUTANT WITH SER 229 REPLACED BY ALA, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE==
|PDB= 1uxy |SIZE=350|CAPTION= <scene name='initialview01'>1uxy</scene>, resolution 1.80&Aring;
<StructureSection load='1uxy' size='340' side='right'caption='[[1uxy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=EPU:URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL)+BUTYRIC+ACID'>EPU</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
<table><tr><td colspan='2'>[[1uxy]] is a 1 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=1UXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UXY FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylmuramate_dehydrogenase UDP-N-acetylmuramate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.158 1.1.1.158] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPU:URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL)+BUTYRIC+ACID'>EPU</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uxy OCA], [https://pdbe.org/1uxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uxy RCSB], [https://www.ebi.ac.uk/pdbsum/1uxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uxy ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uxy OCA], [http://www.ebi.ac.uk/pdbsum/1uxy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uxy RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/MURB_ECOLI MURB_ECOLI] Cell wall formation.
 
== Evolutionary Conservation ==
'''MURB MUTANT WITH SER 229 REPLACED BY ALA, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ux/1uxy_consurf.spt"</scriptWhenChecked>
MurB catalyzes the second committed step in the synthesis of peptidoglycan, a key component of the bacterial cell wall. The crystal structures of both a S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine were solved and refined at 1.8 A resolution. The single point mutation of residue 229 from serine to alanine eliminated a hydroxyl group which has previously been proposed to play a critical role as a proton donor during the second half-reaction of MurB, namely, reoxidation of FADH2 and reduction of the enolpyruvyl substrate. The mutation also resulted in the loss of the water molecule-hydrogen bonded to the serine hydroxyl in the wild-type structure changing the hydrogen-bonding network with in the active site. Comparison of the wild-type and S229A mutant structures confirms that the dramatic kinetic defect of an approximately 10(7)-fold decrease observed for the Ser 229 Ala mutant in the second half-reaction [Benson, T.E., Walsh, C.T., &amp; Massey, V. (1997) Biochemistry 36, 796-805] is a direct result of the loss of the serine hydroxyl moiety rather than other nonspecific active-site changes or general structural defects.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1UXY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UXY OCA].  
</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=1uxy ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution., Benson TE, Walsh CT, Hogle JM, Biochemistry. 1997 Jan 28;36(4):806-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9020778 9020778]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: UDP-N-acetylmuramate dehydrogenase]]
[[Category: Benson TE]]
[[Category: Benson, T E.]]
[[Category: Hogle JM]]
[[Category: Hogle, J M.]]
[[Category: Walsh CT]]
[[Category: Walsh, C T.]]
[[Category: cell division]]
[[Category: cell wall]]
[[Category: fad]]
[[Category: flavoprotein]]
[[Category: nadp]]
[[Category: oxidoreductase]]
[[Category: peptidoglycan synthesis]]
 
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Retrieved from "https://proteopedia.org/1uxy"