4qvh: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein==
<StructureSection load='4qvh' size='340' side='right' caption='[[4qvh]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qvh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QVH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4qvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qvh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qvh RCSB], [http://www.ebi.ac.uk/pdbsum/4qvh PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phosphopantetheinyl transferases (PPTases) are key enzymes in the assembly-line production of complex molecules such as fatty acids, polyketides and polypeptides, where they activate acyl or peptidyl carrier proteins, transferring a 4'-phosphopantetheinyl moiety from coenzyme A (CoA) to a reactive serine residue on the carrier protein. The human pathogen Mycobacterium tuberculosis encodes two PPTases, both essential and therefore attractive drug targets. We report the structure of the type-II PPTase PptT, obtained from crystals of a fusion protein with maltose binding protein. The structure, at 1.75A resolution (R=0.156, Rfree=0.191), reveals an alpha/beta fold broadly similar to other type-II PPTases, but with differences in peripheral structural elements. A bound CoA is clearly defined with its pantetheinyl arm tucked into a hydrophobic pocket. Interactions involving the CoA diphosphate, bound Mg2+ and three active site acidic side chains suggest a plausible pathway for proton transfer during catalysis.


The entry 4qvh is ON HOLD  until Paper Publication
Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein.,Jung J, Bashiri G, Johnston JM, Brown AS, Ackerley DF, Baker EN J Struct Biol. 2014 Oct 18;188(3):274-278. doi: 10.1016/j.jsb.2014.10.004. PMID:25450595<ref>PMID:25450595</ref>


Authors: Jung, J., Bashiri, G., Johnston, J.M., Baker, E.N.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of the essential Mycobacterium tuberculosis phosphopantetheinyl transferase PptT, solved as a fusion protein with maltose binding protein
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Baker, E N]]
[[Category: Bashiri, G]]
[[Category: Johnston, J M]]
[[Category: Jung, J]]
[[Category: A/b-fold]]
[[Category: Acyl carrier protein]]
[[Category: Peptidyl carrier protein]]
[[Category: Phosphopantetheinyl transferase]]
[[Category: Transferase]]
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