4ns3: Difference between revisions
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''' | ==Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis bound with NAD and cobalamin== | ||
<StructureSection load='4ns3' size='340' side='right' caption='[[4ns3]], [[Resolution|resolution]] 2.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ns3]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NS3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NS3 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lem|4lem]]</td></tr> | |||
<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> | |||
<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=4ns3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ns3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ns3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ns3 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The use of small molecules as "silver bullets" that can bind to generate crosslinks between protein molecules has been advanced as a powerful means of enhancing success in protein crystallization (McPherson and Cudney, 2006). We have explored this approach in attempts to overcome an order-disorder phenomenon that complicated the structural analysis of the enzyme Delta1-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis (P5CDH, Mtb-PruA). Using the Silver Bullets Bio screen, we obtained new crystal packing using cobalamin as a co-crystallization agent. This crystal form did not display the order-disorder phenomenon previously encountered. Solution of the crystal structure showed that cobalamin molecules are present in the crystal contacts. Although the cobalamin binding probably does not have physiological relevance, it reflects similarities in the nucleotide-binding region of Mtb-PruA, with the nucleotide loop of cobalamin sharing the binding site for the adenine moiety of NAD+. | |||
Use of a "silver bullet" to resolve crystal lattice dislocation disorder: A cobalamin complex of Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis.,Lagautriere T, Bashiri G, Baker EN J Struct Biol. 2014 Dec 31. pii: S1047-8477(14)00281-0. doi:, 10.1016/j.jsb.2014.12.007. PMID:25557497<ref>PMID:25557497</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: 1-pyrroline-5-carboxylate dehydrogenase]] | |||
[[Category: Baker, E N]] | |||
[[Category: Bashiri, G]] | [[Category: Bashiri, G]] | ||
[[Category: Lagautriere, T]] | [[Category: Lagautriere, T]] | ||
[[Category: | [[Category: Dehydrogenase]] | ||
[[Category: Dehydrogenation]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Rossmann fold]] | |||
Revision as of 16:37, 14 January 2015
Crystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis bound with NAD and cobalaminCrystal structure of the Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis bound with NAD and cobalamin
Structural highlights
Publication Abstract from PubMedThe use of small molecules as "silver bullets" that can bind to generate crosslinks between protein molecules has been advanced as a powerful means of enhancing success in protein crystallization (McPherson and Cudney, 2006). We have explored this approach in attempts to overcome an order-disorder phenomenon that complicated the structural analysis of the enzyme Delta1-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis (P5CDH, Mtb-PruA). Using the Silver Bullets Bio screen, we obtained new crystal packing using cobalamin as a co-crystallization agent. This crystal form did not display the order-disorder phenomenon previously encountered. Solution of the crystal structure showed that cobalamin molecules are present in the crystal contacts. Although the cobalamin binding probably does not have physiological relevance, it reflects similarities in the nucleotide-binding region of Mtb-PruA, with the nucleotide loop of cobalamin sharing the binding site for the adenine moiety of NAD+. Use of a "silver bullet" to resolve crystal lattice dislocation disorder: A cobalamin complex of Delta-pyrroline-5-carboxylate dehydrogenase from Mycobacterium tuberculosis.,Lagautriere T, Bashiri G, Baker EN J Struct Biol. 2014 Dec 31. pii: S1047-8477(14)00281-0. doi:, 10.1016/j.jsb.2014.12.007. PMID:25557497[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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