1hyh
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1hyh |SIZE=350|CAPTION= <scene name='initialview01'>1hyh</scene>, resolution 2.2Å | |PDB= 1hyh |SIZE=350|CAPTION= <scene name='initialview01'>1hyh</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/L-lactate_dehydrogenase L-lactate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.27 1.1.1.27] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hyh OCA], [http://www.ebi.ac.uk/pdbsum/1hyh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hyh RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Niefind, K.]] | [[Category: Niefind, K.]] | ||
[[Category: Schomburg, D.]] | [[Category: Schomburg, D.]] | ||
| - | [[Category: NAD]] | ||
| - | [[Category: SO4]] | ||
[[Category: l-2-hydroxycarboxylate dehydrogenase]] | [[Category: l-2-hydroxycarboxylate dehydrogenase]] | ||
[[Category: l-lactate dehydrogenase]] | [[Category: l-lactate dehydrogenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:01 2008'' |
Revision as of 18:12, 30 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | L-lactate dehydrogenase, with EC number 1.1.1.27 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF L-2-HYDROXYISOCAPROATE DEHYDROGENASE FROM LACTOBACILLUS CONFUSUS AT 2.2 ANGSTROMS RESOLUTION-AN EXAMPLE OF STRONG ASYMMETRY BETWEEN SUBUNITS
Overview
L-2-Hydroxyisocaproate dehydrogenase (L-HicDH) from Lactobacillus confusus, a homotetramer with a molecular mass of 33 kDa per subunit, belongs to the protein family of the NAD(+)-dependent L-2-hydroxycarboxylate dehydrogenases. L-HicDH was crystallized with ammonium sulphate as precipitant in the presence of NAD+. The crystals belong to the trigonal space group P3(2)21, with a = 135.9 A and c = 205.9 A, and diffract X-rays to 2.2 A resolution. The crystal structure was solved by Patterson search and molecular replacement techniques and refined to an R-value of 21.4% (2.2 to 8 A). The final structure model contains one NAD+ molecule and one sulphate ion per subunit, with 309 water molecules. An unusual feature of this crystal structure is the deviation of the protein subunits from non-crystallographic symmetry, which is so strong that it can be detected globally by self-rotation calculations in reciprocal space. This asymmetry is especially pronounced in the environment of the active site; it is reflected also in the nicotinamide conformation of NAD+ and allows some conclusions to be drawn about the catalytic mechanism. In this context, an "inner active site loop" is identified as a structural element of fundamental functional importance. Furthermore, with knowledge of the crystal structure of L-HicDH the differences in substrate specificity between L-HicDH and the L-lactate dehydrogenases can be partly explained.
About this Structure
1HYH is a Single protein structure of sequence from Weissella confusa. Full crystallographic information is available from OCA.
Reference
Crystal structure of L-2-hydroxyisocaproate dehydrogenase from Lactobacillus confusus at 2.2 A resolution. An example of strong asymmetry between subunits., Niefind K, Hecht HJ, Schomburg D, J Mol Biol. 1995 Aug 11;251(2):256-81. PMID:7643402
Page seeded by OCA on Sun Mar 30 21:12:01 2008
