6w98

<table><tr><td colspan='2'>[[6w98]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Escherichia_coli_(strain_k12) Escherichia coli (strain k12)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6W98 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6W98 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6OU:[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl]+(~{Z})-octadec-9-enoate'>6OU</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6w98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6w98 OCA], [http://pdbe.org/6w98 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6w98 RCSB], [http://www.ebi.ac.uk/pdbsum/6w98 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6w98 ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/ACP_ECOLI ACP_ECOLI]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217]

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== Publication Abstract from PubMed ==

Mycobacterium tuberculosis causes tuberculosis, a disease that kills over 1 million people each year. Its cell envelope is a common antibiotic target and has a unique structure due, in part, to two lipidated polysaccharides-arabinogalactan and lipoarabinomannan. Arabinofuranosyltransferase D (AftD) is an essential enzyme involved in assembling these glycolipids. We present the 2.9-A resolution structure of M. abscessus AftD, determined by single-particle cryo-electron microscopy. AftD has a conserved GT-C glycosyltransferase fold and three carbohydrate-binding modules. Glycan array analysis shows that AftD binds complex arabinose glycans. Additionally, AftD is non-covalently complexed with an acyl carrier protein (ACP). 3.4- and 3.5-A structures of a mutant with impaired ACP binding reveal a conformational change, suggesting that ACP may regulate AftD function. Mutagenesis experiments using a conditional knockout constructed in M. smegmatis confirm the essentiality of the putative active site and the ACP binding for AftD function.

 

== References ==

[[Category: Archer, M]]

[[Category: Athayde, D]]

[[Category: Brunton, R]]

[[Category: Carragher, B]]

[[Category: Catalao, M J]]

[[Category: Clarke, O B]]

[[Category: Dandey, V P]]

[[Category: Giacometti, S I]]

[[Category: Kloss, B]]

[[Category: Lowary, T L]]

[[Category: Mancia, F]]

[[Category: Niederweis, M]]

[[Category: Pimentel, M]]

[[Category: Potter, C S]]

[[Category: Raczkowski, A M]]

[[Category: Rodrigues, J]]

[[Category: Rosario, A L]]

[[Category: Tan, Y Z]]

[[Category: Wei, H]]

[[Category: Zhang, L]]

[[Category: Zheng, R B]]

[[Category: Single-particle cryo-electron microscopy]]