4cl3

1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus

spinqualitylabelsall models 4cl3, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cl3 is a 2 chain structure with sequence from Chloroflexus aurantiacus Y-400-fl. This structure supersedes the now removed PDB entry 4bgt. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.699Å Ligands: ACT, CD, CL, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MDH_CHLSY Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity). Publication Abstract from PubMed Protein-solvent interactions govern the behaviors of proteins isolated from extreme halophiles. In this work, we compared the solvent envelopes of two orthologous tetrameric malate dehydrogenases (MalDHs) from halophilic and non-halophilic bacteria. The crystal structure of the MalDH from the non-halophilic bacterium Chloroflexus aurantiacus (Ca MalDH) solved, de novo, at 1.7 A resolution exhibits numerous water molecules in its solvation shell. We observed that a large number of these water molecules are arranged in pentagonal polygons in the first hydration shell of Ca MalDH. Some of them are clustered in large networks, which cover non-polar amino acid surface. The crystal structure of MalDH from the extreme halophilic bacterium Salinibacter ruber (Sr) solved at 1.55 A resolution shows that its surface is strongly enriched in acidic amino acids. The structural comparison of these two models is the first direct observation of the relative impact of acidic surface enrichment on the water structure organization between a halophilic protein and its non-adapted counterpart. The data show that surface acidic amino acids disrupt pentagonal water networks in the hydration shell. These crystallographic observations are discussed with respect to halophilic protein behaviors in solution. An experimental point of view on hydration/solvation in halophilic proteins.,Talon R, Coquelle N, Madern D, Girard E Front Microbiol. 2014 Feb 21;5:66. doi: 10.3389/fmicb.2014.00066. eCollection, 2014. PMID:24600446 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Malate Dehydrogenase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA