4ihi

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==Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis bound with NAD==
==Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis bound with NAD==
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<StructureSection load='4ihi' size='340' side='right' caption='[[4ihi]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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<StructureSection load='4ihi' size='340' side='right'caption='[[4ihi]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ihi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IHI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IHI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ihi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IHI FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4idm|4idm]], [[4ids|4ids]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/1-pyrroline-5-carboxylate_dehydrogenase 1-pyrroline-5-carboxylate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.12 1.5.1.12] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ihi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihi OCA], [https://pdbe.org/4ihi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ihi RCSB], [https://www.ebi.ac.uk/pdbsum/4ihi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ihi ProSAT]</span></td></tr>
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<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=4ihi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ihi RCSB], [http://www.ebi.ac.uk/pdbsum/4ihi PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O50443_MYCTU O50443_MYCTU]
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The proline-utilization pathway in Mycobacterium tuberculosis (Mtb) has recently been identified as an important factor in Mtb persistence in vivo, suggesting that this pathway could be a valuable therapeutic target against tuberculosis (TB). In Mtb, two distinct enzymes perform the conversion of proline into glutamate: the first step is the oxidation of proline into Delta(1)-pyrroline-5-carboxylic acid (P5C) by the flavoenzyme proline dehydrogenase (PruB), and the second reaction involves converting the tautomeric form of P5C (glutamate-gamma-semialdehyde) into glutamate using the NAD(+)-dependent Delta(1)-pyrroline-5-carboxylic dehydrogenase (PruA). Here, the three-dimensional structures of Mtb-PruA, determined by X-ray crystallography, in the apo state and in complex with NAD(+) are described at 2.5 and 2.1 A resolution, respectively. The structure reveals a conserved NAD(+)-binding mode, common to other related enzymes. Species-specific conformational differences in the active site, however, linked to changes in the dimer interface, suggest possibilities for selective inhibition of Mtb-PruA despite its reasonably high sequence identity to other PruA enzymes. Using recombinant PruA and PruB, the proline-utilization pathway in Mtb has also been reconstituted in vitro. Functional validation using a novel NMR approach has demonstrated that the PruA and PruB enzymes are together sufficient to convert proline to glutamate, the first such demonstration for monofunctional proline-utilization enzymes.
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Characterization of the proline-utilization pathway in Mycobacterium tuberculosis through structural and functional studies.,Lagautriere T, Bashiri G, Paterson NG, Berney M, Cook GM, Baker EN Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):968-80. doi:, 10.1107/S1399004713034391. Epub 2014 Mar 19. PMID:24699642<ref>PMID:24699642</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
==See Also==
*[[Pyrroline-5-carboxylate dehydrogenase|Pyrroline-5-carboxylate dehydrogenase]]
*[[Pyrroline-5-carboxylate dehydrogenase|Pyrroline-5-carboxylate dehydrogenase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 1-pyrroline-5-carboxylate dehydrogenase]]
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[[Category: Large Structures]]
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[[Category: Baker, E N]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Bashiri, G]]
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[[Category: Baker EN]]
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[[Category: Lagautriere, T]]
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[[Category: Bashiri G]]
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[[Category: Dehydrogenation]]
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[[Category: Lagautriere T]]
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[[Category: Oxidoreductase]]
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[[Category: Pyrroline-5-carboxylate dehtdrogenase]]
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[[Category: Pyrroline-5-carboxylic acid]]
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[[Category: Rossmann fold]]
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Current revision

Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis bound with NAD

PDB ID 4ihi

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