6hwr
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Red kidney bean purple acid phosphatase in complex with adenosine divanadate== | |
| + | <StructureSection load='6hwr' size='340' side='right'caption='[[6hwr]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6hwr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Phaseolus_vulgaris Phaseolus vulgaris]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4kkz 4kkz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HWR FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</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=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H1Q:adenosine+divanadate'>H1Q</scene>, <scene name='pdbligand=H1T:[[[[bis($l^{1}-oxidanyl)-[$l^{1}-oxidanyl-[tris($l^{1}-oxidanyl)vanadiooxy]vanadio]oxy-vanadio]oxy-bis($l^{1}-oxidanyl)vanadio]oxy-oxidanylidene-vanadio]-[bis($l^{1}-oxidanyl)vanadio]-$l^{3}-oxidanyl]-tetrakis($l^{1}-oxidanyl)vanadium'>H1T</scene>, <scene name='pdbligand=H1W:pentakis(oxidanyl)vanadium'>H1W</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VN3:VANADATE+ION'>VN3</scene>, <scene name='pdbligand=VV6:[[[[bis(oxidanyl)-[tris(oxidanyl)vanadiooxy]vanadio]oxy-bis(oxidanyl)vanadio]-oxidanylidene-vanadio]oxy-oxidanyl-vanadio]oxy-tetrakis(oxidanyl)vanadium'>VV6</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6hwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hwr OCA], [https://pdbe.org/6hwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hwr RCSB], [https://www.ebi.ac.uk/pdbsum/6hwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hwr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PPAF_PHAVU PPAF_PHAVU] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Purple acid phosphatases (PAPs) are members of the large family of metallohydrolases, a group of enzymes that perform a wide range of biological functions, while employing a highly conserved catalytic mechanism. PAPs are found in plants, animals and fungi; in humans they play an important role in bone turnover and are thus of interest for developing treatments for osteoporosis. The majority of metallohydrolases use a metal-bound hydroxide to initiate catalysis, which leads to the formation of a proposed five-coordinate oxyphosphorane species in the transition state. In this work, we crystallized PAP from red kidney beans (rkbPAP) in the presence of both adenosine and vanadate. The in crystallo-formed vanadate analogue of ADP provides detailed insight into the binding mode of a PAP substrate, captured in a structure that mimics the putative fivecoordinate transition state. Our observations not only provide unprecedented insight into the mechanism of metallohydrolases, but might also guide the structure-based design of inhibitors for application in the treatment of several human illnesses. | ||
| - | + | The Binding Mode of an ADP Analogue to a Metallohydrolase Mimics the Likely Transition State.,Feder D, Gahan LR, McGeary RP, Guddat LW, Schenk G Chembiochem. 2019 Feb 4. doi: 10.1002/cbic.201900077. PMID:30719821<ref>PMID:30719821</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Feder | + | <div class="pdbe-citations 6hwr" style="background-color:#fffaf0;"></div> |
| - | [[Category: Gahan | + | |
| - | [[Category: | + | ==See Also== |
| - | [[Category: | + | *[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]] |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Phaseolus vulgaris]] | ||
| + | [[Category: Feder D]] | ||
| + | [[Category: Gahan LR]] | ||
| + | [[Category: Guddat LW]] | ||
| + | [[Category: McGeary RP]] | ||
| + | [[Category: Schenk G]] | ||
Current revision
Red kidney bean purple acid phosphatase in complex with adenosine divanadate
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