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| | ==Crystal structure of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDS) complex with NAD and phosphate== | | ==Crystal structure of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDS) complex with NAD and phosphate== |
| - | <StructureSection load='3h9e' size='340' side='right' caption='[[3h9e]], [[Resolution|resolution]] 1.72Å' scene=''> | + | <StructureSection load='3h9e' size='340' side='right'caption='[[3h9e]], [[Resolution|resolution]] 1.72Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3h9e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3H9E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3h9e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H9E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GAPD2, GAPDH2, GAPDHS, GAPDS, HSD-35, HSD35 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.12 1.2.1.12] </span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h9e OCA], [https://pdbe.org/3h9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h9e RCSB], [https://www.ebi.ac.uk/pdbsum/3h9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h9e ProSAT]</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=3h9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h9e OCA], [http://pdbe.org/3h9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h9e RCSB], [http://www.ebi.ac.uk/pdbsum/3h9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h9e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G3PT_HUMAN 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). | + | [https://www.uniprot.org/uniprot/G3PT_HUMAN 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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Glyceraldehyde-3-Phosphate Dehydrogenase|Glyceraldehyde-3-Phosphate Dehydrogenase]] | + | *[[Glyceraldehyde-3-phosphate dehydrogenase 3D structures|Glyceraldehyde-3-phosphate dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Arrowsmith, C H]] | + | [[Category: Large Structures]] |
| - | [[Category: Bountra, C]] | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Bray, J E]] | + | [[Category: Bountra C]] |
| - | [[Category: Chaikuad, A]] | + | [[Category: Bray JE]] |
| - | [[Category: Cocking, R]] | + | [[Category: Chaikuad A]] |
| - | [[Category: Delft, F von]]
| + | [[Category: Cocking R]] |
| - | [[Category: Edwards, A M]] | + | [[Category: Edwards AM]] |
| - | [[Category: Oppermann, U]] | + | [[Category: Oppermann U]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Shafqat N]] |
| - | [[Category: Shafqat, N]] | + | [[Category: Weigelt J]] |
| - | [[Category: Weigelt, J]] | + | [[Category: Yue W]] |
| - | [[Category: Yue, W]] | + | [[Category: Von Delft F]] |
| - | [[Category: Glycolysis]] | + | |
| - | [[Category: Nad]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Sgc]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chaikuad A, Shafqat N, Al-Mokhtar R, Cameron G, Clarke AR, Brady L, Oppermann U, Frayne J, Yue WW. Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS. Biochem J. 2011 Jan 26. PMID:21269272 doi:10.1042/BJ20101442
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