4mqy: Difference between revisions

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{{STRUCTURE_4mqy|  PDB=4mqy  |  SCENE=  }}
===Crystal Structure of the Escherichia coli LpxC/LPC-138 complex===
{{ABSTRACT_PUBMED_24117400}}


==Function==
==Crystal Structure of the Escherichia coli LpxC/LPC-138 complex==
[[http://www.uniprot.org/uniprot/D5CV28_ECOKI D5CV28_ECOKI]] Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (By similarity).[HAMAP-Rule:MF_00388][SAAS:SAAS004463_004_013136]
<StructureSection load='4mqy' size='340' side='right'caption='[[4mqy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mqy]] 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=4MQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MQY 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]] 2.005&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2CW:4-[4-(4-AMINOPHENYL)BUTA-1,3-DIYN-1-YL]-N-[(2S,3R)-3-HYDROXY-2-METHYL-1-NITROSO-1-OXOBUTAN-2-YL]BENZAMIDE'>2CW</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UKW:4-ETHYNYL-N-[(1S,2R)-2-HYDROXY-1-(OXOCARBAMOYL)PROPYL]BENZAMIDE'>UKW</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4mqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mqy OCA], [https://pdbe.org/4mqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mqy RCSB], [https://www.ebi.ac.uk/pdbsum/4mqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mqy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LPXC_ECOLI LPXC_ECOLI] Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.[HAMAP-Rule:MF_00388]<ref>PMID:10026271</ref> <ref>PMID:8530464</ref> <ref>PMID:8824222</ref> <ref>PMID:18289052</ref>


==About this Structure==
==See Also==
[[4mqy]] is a 1 chain structure with 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=4MQY OCA].
*[[UDP-3-O-acyl-N-acetylglucosamine deacetylase|UDP-3-O-acyl-N-acetylglucosamine deacetylase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:024117400</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Lee, C J.]]
[[Category: Large Structures]]
[[Category: Najeeb, J.]]
[[Category: Lee C-J]]
[[Category: Zhou, P.]]
[[Category: Najeeb J]]
[[Category: Acyl udp-glcnac]]
[[Category: Zhou P]]
[[Category: Antibiotic]]
[[Category: Baab sandwich]]
[[Category: Deacetylation]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Hydroxamate]]
[[Category: Lipid a biosynthesis]]
[[Category: Lipid a synthesis]]
[[Category: Lpc-138]]
[[Category: Lpxc]]

Latest revision as of 15:28, 1 March 2024

Crystal Structure of the Escherichia coli LpxC/LPC-138 complexCrystal Structure of the Escherichia coli LpxC/LPC-138 complex

Structural highlights

4mqy is a 1 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 2.005Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LPXC_ECOLI Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.[HAMAP-Rule:MF_00388][1] [2] [3] [4]

See Also

References

  1. ↑ Jackman JE, Raetz CR, Fierke CA. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme. Biochemistry. 1999 Feb 9;38(6):1902-11. doi: 10.1021/bi982339s. PMID:10026271 doi:http://dx.doi.org/10.1021/bi982339s
  2. ↑ Young K, Silver LL, Bramhill D, Cameron P, Eveland SS, Raetz CR, Hyland SA, Anderson MS. The envA permeability/cell division gene of Escherichia coli encodes the second enzyme of lipid A biosynthesis. UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase. J Biol Chem. 1995 Dec 22;270(51):30384-91. doi: 10.1074/jbc.270.51.30384. PMID:8530464 doi:http://dx.doi.org/10.1074/jbc.270.51.30384
  3. ↑ Sorensen PG, Lutkenhaus J, Young K, Eveland SS, Anderson MS, Raetz CR. Regulation of UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase in Escherichia coli. The second enzymatic step of lipid a biosynthesis. J Biol Chem. 1996 Oct 18;271(42):25898-905. doi: 10.1074/jbc.271.42.25898. PMID:8824222 doi:http://dx.doi.org/10.1074/jbc.271.42.25898
  4. ↑ Barb AW, Zhou P. Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis. Curr Pharm Biotechnol. 2008 Feb;9(1):9-15. PMID:18289052

4mqy, resolution 2.00Å

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