View source for 4j72

==Crystal Structure of polyprenyl-phosphate N-acetyl hexosamine 1-phosphate transferase==
<StructureSection load='4j72' size='340' side='right' caption='[[4j72]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4j72]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aq_053, mraY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospho-N-acetylmuramoyl-pentapeptide-transferase Phospho-N-acetylmuramoyl-pentapeptide-transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.13 2.7.8.13] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j72 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j72 RCSB], [http://www.ebi.ac.uk/pdbsum/4j72 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://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;">
== Publication Abstract from PubMed ==
MraY (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<ref>PMID:23990562</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aquifex aeolicus]]
[[Category: Phospho-N-acetylmuramoyl-pentapeptide-transferase]]
[[Category: Chung, B C]]
[[Category: Gillespie, R A]]
[[Category: Guan, Z]]
[[Category: Hong, J]]
[[Category: Kwon, D Y]]
[[Category: Lee, S Y]]
[[Category: Zhou, P]]
[[Category: Alpha-helical membrane protein]]
[[Category: Magnesium binding]]
[[Category: Membrane]]
[[Category: Membrane enzyme]]
[[Category: Transferase]]
[[Category: Udp-murnac-pentapeptide binding]]
[[Category: Undecaprenyl phosphate binding]]