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| | <StructureSection load='4zev' size='340' side='right'caption='[[4zev]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4zev' size='340' side='right'caption='[[4zev]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zev]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZEV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZEV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zev]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZEV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=M6P:ALPHA-D-MANNOSE-6-PHOSPHATE'>M6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zew|4zew]], [[4zex|4zex]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M6P:ALPHA-D-MANNOSE-6-PHOSPHATE'>M6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF10_0325 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</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=4zev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zev OCA], [https://pdbe.org/4zev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zev RCSB], [https://www.ebi.ac.uk/pdbsum/4zev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zev 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=4zev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zev OCA], [http://pdbe.org/4zev PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zev RCSB], [http://www.ebi.ac.uk/pdbsum/4zev PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zev ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8IJ74_PLAF7 Q8IJ74_PLAF7] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Plaf7]] | + | [[Category: Plasmodium falciparum 3D7]] |
| - | [[Category: Park, J]] | + | [[Category: Park J]] |
| - | [[Category: Tolia, N H]] | + | [[Category: Tolia NH]] |
| - | [[Category: C2 had]]
| + | |
| - | [[Category: Haloacid-dehalogenase]]
| + | |
| - | [[Category: Mannose-6-phosphate]]
| + | |
| - | [[Category: Sugar phosphatase]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
Q8IJ74_PLAF7
Publication Abstract from PubMed
Haloacid dehalogenases (HADs) are a large enzyme superfamily of more than 500,000 members with roles in numerous metabolic pathways. Plasmodium falciparum HAD1 (PfHAD1) is a sugar phosphatase that regulates the methylerythritol phosphate (MEP) pathway for isoprenoid synthesis in malaria parasites. However, the structural determinants for diverse substrate recognition by HADs are unknown. Here, crystal structures were determined of PfHAD1 in complex with three sugar phosphates selected from a panel of diverse substrates that it utilizes. Cap-open and cap-closed conformations are observed, with cap closure facilitating substrate binding and ordering. These structural changes define the role of cap movement within the major subcategory of C2 HAD enzymes. The structures of an HAD bound to multiple substrates identifies binding and specificity-determining residues that define the structural basis for substrate recognition and catalysis within the HAD superfamily. While the substrate-binding region of the cap domain is flexible in the open conformations, this region becomes ordered and makes direct interactions with the substrate in the closed conformations. These studies further inform the structural and biochemical basis for catalysis within a large superfamily of HAD enzymes with diverse functions.
Cap-domain closure enables diverse substrate recognition by the C2-type haloacid dehalogenase-like sugar phosphatase Plasmodium falciparum HAD1.,Park J, Guggisberg AM, Odom AR, Tolia NH Acta Crystallogr D Biol Crystallogr. 2015 Sep;71(Pt 9):1824-34. doi:, 10.1107/S1399004715012067. Epub 2015 Aug 25. PMID:26327372[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park J, Guggisberg AM, Odom AR, Tolia NH. Cap-domain closure enables diverse substrate recognition by the C2-type haloacid dehalogenase-like sugar phosphatase Plasmodium falciparum HAD1. Acta Crystallogr D Biol Crystallogr. 2015 Sep;71(Pt 9):1824-34. doi:, 10.1107/S1399004715012067. Epub 2015 Aug 25. PMID:26327372 doi:http://dx.doi.org/10.1107/S1399004715012067
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