4j72: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase== | ==Crystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase== | ||
<StructureSection load='4j72' size='340' side='right' caption='[[4j72]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='4j72' size='340' side='right'caption='[[4j72]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4j72]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4j72]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J72 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=4j72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j72 OCA], [https://pdbe.org/4j72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j72 RCSB], [https://www.ebi.ac.uk/pdbsum/4j72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j72 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/MRAY_AQUAE MRAY_AQUAE] First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 24: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aquifex aeolicus | [[Category: Aquifex aeolicus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chung | [[Category: Chung BC]] | ||
[[Category: Gillespie | [[Category: Gillespie RA]] | ||
[[Category: Guan | [[Category: Guan Z]] | ||
[[Category: Hong | [[Category: Hong J]] | ||
[[Category: Kwon | [[Category: Kwon DY]] | ||
[[Category: Lee | [[Category: Lee SY]] | ||
[[Category: Zhou | [[Category: Zhou P]] | ||
Revision as of 13:55, 24 November 2022
Crystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferaseCrystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase
Structural highlights
FunctionMRAY_AQUAE First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan (By similarity). Publication Abstract from PubMedMraY (phospho-MurNAc-pentapeptide translocase) is an integral membrane enzyme that catalyzes an essential step of bacterial cell wall biosynthesis: the transfer of the peptidoglycan precursor phospho-MurNAc-pentapeptide to the lipid carrier undecaprenyl phosphate. MraY has long been considered a promising target for the development of antibiotics, but the lack of a structure has hindered mechanistic understanding of this critical enzyme and the enzyme superfamily in general. The superfamily includes enzymes involved in bacterial lipopolysaccharide/teichoic acid formation and eukaryotic N-linked glycosylation, modifications that are central in many biological processes. We present the crystal structure of MraY from Aquifex aeolicus (MraYAA) at 3.3 A resolution, which allows us to visualize the overall architecture, locate Mg(2+) within the active site, and provide a structural basis of catalysis for this class of enzyme. Crystal structure of MraY, an essential membrane enzyme for bacterial cell wall synthesis.,Chung BC, Zhao J, Gillespie RA, Kwon DY, Guan Z, Hong J, Zhou P, Lee SY Science. 2013 Aug 30;341(6149):1012-6. doi: 10.1126/science.1236501. PMID:23990562[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||