3h9e | pdb_00003h9e

Crystal structure of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDS) complex with NAD and phosphate

spinqualitylabelsall models 3h9e, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3h9e is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, NAD, PO4 Gene: GAPD2, GAPDH2, GAPDHS, GAPDS, HSD-35, HSD35 (HUMAN) Activity: Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating), with EC number 1.2.1.12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [G3PT_HUMAN] May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility (By similarity). 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 Human sperm-specific glyceraldehyde-3-phosphate dehydrogenase (hGAPDS) is a glycolytic enzyme essential for the survival of spermatozoa, and constitutes a potential target for non-hormonal contraception. However, enzyme characterization of GAPDS has been hampered by the difficulty in producing soluble recombinant protein. Here, we have over-expressed in E. coli a highly-soluble form of hGAPDS truncated at the N-terminus (hGAPDSN), and crystallized the homo-tetrameric enzyme in two ligand complexes. The hGAPDSN-NAD+-phosphate structure maps the two anion recognition sites within the catalytic pocket that correspond to the conserved Ps site and the newly recognised Pi site identified in other organisms. The hGAPDSN-NAD+-glycerol structure shows serendipitous binding of glycerol at the Ps and new Pi sites, demonstrating the propensity of these anion recognition sites to bind non-physiologically-relevant ligands. A comparison of kinetic profiles between hGAPDSN and its somatic equivalent reveals a moderate 3-fold increase in catalytic efficiency for hGAPDSN. This may be attributable to subtle amino acid substitutions peripheral to the active centre that influence the charge properties and protonation states of catalytic residues. Our data therefore elucidate structural and kinetic features of hGAPDS that might provide insightful information towards inhibitor development. Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS.,Chaikuad A, Shafqat N, Al-Mokhtar R, Cameron G, Clarke AR, Brady L, Oppermann U, Frayne J, Yue WW Biochem J. 2011 Jan 26. PMID:21269272 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glyceraldehyde-3-phosphate dehydrogenase 3D structures

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