3ps7: Difference between revisions
New page: '''Unreleased structure''' The entry 3ps7 is ON HOLD Authors: Kaur, N., Gautam, A., Kumar, S., Singh, A., Singh, N., Sharma, S., Sharma, R., Tewari, R., Singh, T.P. Description: Bioche... |
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The | ==Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa== | ||
<StructureSection load='3ps7' size='340' side='right'caption='[[3ps7]], [[Resolution|resolution]] 2.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ps7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PS7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PS7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGO:S-1,2-PROPANEDIOL'>PGO</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ps7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ps7 OCA], [https://pdbe.org/3ps7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ps7 RCSB], [https://www.ebi.ac.uk/pdbsum/3ps7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ps7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DAPA_PSEAE DAPA_PSEAE] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).<ref>PMID:21396954</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The intracellular enzyme dihydrodipicolinate synthase (DHDPS, E.C. 4.2.1.52) from Pseudomonas aeruginosa is a potential drug target because it is essential for the growth of bacteria while it is absent in humans. Therefore, in order to design new compounds using structure based approach for inhibiting the function of DHDPS from P. aeruginosa (Ps), we have cloned, characterized biochemically and biophysically and have determined its three-dimensional structure. The gene encoding DHDPS (dapA) was cloned in a vector pET-28c(+) and the recombinant protein was overexpressed in the Escherichia coli host. The K(m) values of the recombinant enzyme estimated for the substrates, pyruvate and (S)-aspartate-beta-semialdehyde [(S)-ASA] were found to be 0.90+/-0.13 mM and 0.17+/-0.02 mM, respectively. The circular dichroism studies showed that the enzyme adopts a characteristic beta/alpha conformation which is retained up to 65 degrees C. The fluorescence data indicated the presence of exposed tryptophan residues in the enzyme. The three-dimensional structure determination showed that DHDPS forms a homodimer which is stabilized by several hydrogen bonds and van der Waals forces at the interface. The active site formed with residues Thr44, Tyr107 and Tyr133 is found to be stereochemically suitable for catalytic function. It may be noted that Tyr107 of the catalytic triad belongs to the partner molecule in the dimer. The structure of the complex of PsDHDPS with (S)-lysine determined at 2.65 A resolution revealed the positions of three lysine molecules bound to the protein. | |||
Biochemical studies and crystal structure determination of dihydrodipicolinate synthase from Pseudomonas aeruginosa.,Kaur N, Gautam A, Kumar S, Singh A, Singh N, Sharma S, Sharma R, Tewari R, Singh TP Int J Biol Macromol. 2011 Jun 1;48(5):779-87. Epub 2011 Mar 10. PMID:21396954<ref>PMID:21396954</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ps7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa PAO1]] | |||
[[Category: Gautam A]] | |||
[[Category: Kaur N]] | |||
[[Category: Kumar S]] | |||
[[Category: Sharma R]] | |||
[[Category: Sharma S]] | |||
[[Category: Singh A]] | |||
[[Category: Singh N]] | |||
[[Category: Singh TP]] | |||
[[Category: Tewari R]] |