3hhp: Difference between revisions

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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=3hhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hhp RCSB], [http://www.ebi.ac.uk/pdbsum/3hhp PDBsum]</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=3hhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hhp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hhp RCSB], [http://www.ebi.ac.uk/pdbsum/3hhp PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/MDH_ECOLI MDH_ECOLI]] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_01516]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 15:35, 25 December 2014

Malate dehydrogenase open conformationMalate dehydrogenase open conformation

Structural highlights

3hhp is a 4 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:mdh, b3236, JW3205 (Escherichia coli K-12)
Activity:Malate dehydrogenase, with EC number 1.1.1.37
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[MDH_ECOLI] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_01516]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 A resolution. The crystals belonged to space group C2, with unit-cell parameters a = 146.0, b = 52.0, c = 168.9 A, beta = 102.2 degrees. The structure was determined with the molecular-replacement pipeline program BALBES and was refined to a final R factor of 18.6% (R(free) = 21.4%). The final model has two dimers in the asymmetric unit. In each dimer one monomer contains the active-site loop in the open conformation, whereas in the opposing monomer the active-site loop is disordered.

Structure of Escherichia coli malate dehydrogenase at 1.45 A resolution.,Zaitseva J, Meneely KM, Lamb AL Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt, 9):866-9. Epub 2009 Aug 20. PMID:19724119[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Zaitseva J, Meneely KM, Lamb AL. Structure of Escherichia coli malate dehydrogenase at 1.45 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt, 9):866-9. Epub 2009 Aug 20. PMID:19724119 doi:10.1107/S1744309109032217

3hhp, resolution 1.45Å

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