6hwr: Difference between revisions

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'''Unreleased structure'''


The entry 6hwr is ON HOLD
==Red kidney bean purple acid phosphatase in complex with adenosine divanadate==
<StructureSection load='6hwr' size='340' side='right'caption='[[6hwr]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hwr]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HWR 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=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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </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=6hwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hwr OCA], [http://pdbe.org/6hwr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hwr RCSB], [http://www.ebi.ac.uk/pdbsum/6hwr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hwr ProSAT]</span></td></tr>
</table>
<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.


Authors: Feder, D., Gahan, L.R., McGeary, R.P., Guddat, L.W., Schenk, G.
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>


Description: Red kidney bean purple acid phosphatase in complex with adenosine divanadate
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6hwr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acid phosphatase]]
[[Category: Large Structures]]
[[Category: Phaseolus vulgaris]]
[[Category: Feder, D]]
[[Category: Feder, D]]
[[Category: Gahan, L.R]]
[[Category: Gahan, L R]]
[[Category: Guddat, L W]]
[[Category: McGeary, R P]]
[[Category: Schenk, G]]
[[Category: Schenk, G]]
[[Category: Mcgeary, R.P]]
[[Category: Catalysis]]
[[Category: Guddat, L.W]]
[[Category: Metal binding protein]]
[[Category: Metallohydrolase]]
[[Category: Osteoporosis]]
[[Category: Purple acid phosphatase]]
[[Category: Transition state]]
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