Proteopedia

1p9b: Difference between revisions

← Older edit
No edit summary
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1p9b.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1p9b", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1p9b|  PDB=1p9b  |  SCENE=  }}
'''Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum'''


==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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1P9B is a [[Single protein]] structure of 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].
</div>
<div class="pdbe-citations 1p9b" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/14729341 14729341]
*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]]
[[Category: Adenylosuccinate synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
[[Category: Single protein]]
[[Category: Anand RP]]
[[Category: Anand, R P.]]
[[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 MR]]
[[Category: Murthy, M R.]]
[[Category: Sumathy K]]
[[Category: Sumathy, K.]]
[[Category: Ligase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:50:43 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/w/1p9b"