1p9b: Difference between revisions

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-[[Image:1p9b.png|left|200px]]
-{{STRUCTURE_1p9b|  PDB=1p9b  |  SCENE=  }}
+==Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum==
+<StructureSection load='1p9b' size='340' side='right'caption='[[1p9b]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1p9b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P9B 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]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=HDA:HADACIDIN'>HDA</scene>, <scene name='pdbligand=IMO:6-O-PHOSPHORYL+INOSINE+MONOPHOSPHATE'>IMO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=1p9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9b OCA], [https://pdbe.org/1p9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p9b RCSB], [https://www.ebi.ac.uk/pdbsum/1p9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p9b ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PURA_PLAFA PURA_PLAFA] Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).<ref>PMID:12071700</ref> <ref>PMID:15500910</ref> <ref>PMID:20654742</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p9/1p9b_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p9b ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+In the absence of the de novo purine nucleotide biosynthetic pathway in parasitic protozoa, purine salvage is of primary importance for parasite survival. Enzymes of the salvage pathway are, therefore, good targets for anti-parasitic drugs. Adenylosuccinate synthetase (AdSS), catalysing the first committed step in the synthesis of AMP from IMP, is a potential target for anti-protozoal chemotherapy. We report here the crystal structure of adenylosuccinate synthetase from the malaria parasite, Plasmodium falciparum, complexed to 6-phosphoryl IMP, GDP, Mg2+ and the aspartate analogue, hadacidin at 2 A resolution. The overall architecture of P. falciparum AdSS (PfAdSS) is similar to the known structures from Escherichia coli, mouse and plants. Differences in substrate interactions seen in this structure provide a plausible explanation for the kinetic differences between PfAdSS and the enzyme from other species. Additional hydrogen bonding interactions of the protein with GDP may account for the ordered binding of substrates to the enzyme. The dimer interface of PfAdSS is also different, with a pronounced excess of positively charged residues. Differences highlighted here provide a basis for the design of species-specific inhibitors of the enzyme.
-===Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum===
+Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum.,Eaazhisai K, Jayalakshmi R, Gayathri P, Anand RP, Sumathy K, Balaram H, Murthy MR J Mol Biol. 2004 Jan 30;335(5):1251-64. PMID:14729341<ref>PMID:14729341</ref>
-{{ABSTRACT_PUBMED_14729341}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1p9b" style="background-color:#fffaf0;"></div>
-[[1p9b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9B OCA].
 ==See Also==
-*[[Adenylosuccinate Synthetase|Adenylosuccinate Synthetase]]
+*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:014729341</ref><references group="xtra"/>
+__TOC__
-[[Category: Adenylosuccinate synthase]]
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Plasmodium falciparum]]
-[[Category: Anand, R P.]]
+[[Category: Anand RP]]
-[[Category: Balaram, H.]]
+[[Category: Balaram H]]
-[[Category: Eaazhisai, K.]]
+[[Category: Eaazhisai K]]
-[[Category: Gayathri, P.]]
+[[Category: Gayathri P]]
-[[Category: Jayalakshmi, R.]]
+[[Category: Jayalakshmi R]]
-[[Category: Murthy, M R.]]
+[[Category: Murthy MR]]
-[[Category: Sumathy, K.]]
+[[Category: Sumathy K]]
-[[Category: Ligase]]