3ckv

<StructureSection load='3ckv' size='340' side='right' caption='[[3ckv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[3ckv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_avium_subsp._paratuberculosis Mycobacterium avium subsp. paratuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CKV FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ckj|3ckj]], [[3ckn|3ckn]], [[3kco|3kco]], [[3kcq|3kcq]]</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ckv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ckv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ckv RCSB], [http://www.ebi.ac.uk/pdbsum/3ckv PDBsum]</span></td></tr>

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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ck/3ckv_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

Glycosyltransferases (GTs) are a large and ubiquitous family of enzymes that specifically transfer sugar moieties to a range of substrates. Mycobacterium tuberculosis contains a large number of GTs, many of which are implicated in cell wall synthesis, yet the majority of these GTs remain poorly characterized. Here, we report the high resolution crystal structures of an essential GT (MAP2569c) from Mycobacterium avium subsp. paratuberculosis (a close homologue of Rv1208 from M. tuberculosis) in its apo- and ligand-bound forms. The structure adopted the GT-A fold and possessed the characteristic DXD motif that coordinated an Mn(2+) ion. Atypical of most GTs characterized to date, MAP2569c exhibited specificity toward the donor substrate, UDP-glucose. The structure of this ligated complex revealed an induced fit binding mechanism and provided a basis for this unique specificity. Collectively, the structural features suggested that MAP2569c may adopt a "retaining" enzymatic mechanism, which has implications for the classification of other GTs in this large superfamily.

Crystal structure of a UDP-glucose-specific glycosyltransferase from a Mycobacterium species.,Fulton Z, McAlister A, Wilce MC, Brammananth R, Zaker-Tabrizi L, Perugini MA, Bottomley SP, Coppel RL, Crellin PK, Rossjohn J, Beddoe T J Biol Chem. 2008 Oct 10;283(41):27881-90. Epub 2008 Jul 30. PMID:18667419<ref>PMID:18667419</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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[[Category: Mycobacterium avium subsp. paratuberculosis]]

[[Category: Marland, Z.]]

[[Category: Rossjohn, J.]]

[[Category: Unknown function]]