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3OYX

Haloferax volcanii Malate Synthase Magnesium/Glyoxylate Complex

Summary for 3OYX
Entry DOI10.2210/pdb3oyx/pdb
Related3OYZ 3PUG
DescriptorMalate synthase, GLYOXYLIC ACID, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordstim barrel, glyoxylate complex, transferase
Biological sourceHaloferax volcanii
Cellular locationCytoplasm : D4GTL2
Total number of polymer chains1
Total formula weight48533.78
Authors
Howard, B.R.,Bracken, C.,Neighbor, A.,Thomas, G.,Lamlenn, K.K.,Schubert, H.L.,Whitby, F.G. (deposition date: 2010-09-24, release date: 2011-06-01, Last modification date: 2024-02-21)
Primary citationBracken, C.D.,Neighbor, A.M.,Lamlenn, K.K.,Thomas, G.C.,Schubert, H.L.,Whitby, F.G.,Howard, B.R.
Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G.
Bmc Struct.Biol., 11:23-23, 2011
Cited by
PubMed Abstract: Malate synthase, one of the two enzymes unique to the glyoxylate cycle, is found in all three domains of life, and is crucial to the utilization of two-carbon compounds for net biosynthetic pathways such as gluconeogenesis. In addition to the main isoforms A and G, so named because of their differential expression in E. coli grown on either acetate or glycolate respectively, a third distinct isoform has been identified. These three isoforms differ considerably in size and sequence conservation. The A isoform (MSA) comprises ~530 residues, the G isoform (MSG) is ~730 residues, and this third isoform (MSH-halophilic) is ~430 residues in length. Both isoforms A and G have been structurally characterized in detail, but no structures have been reported for the H isoform which has been found thus far only in members of the halophilic Archaea.
PubMed: 21569248
DOI: 10.1186/1472-6807-11-23
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.51 Å)
Structure validation

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