2fpp: Difference between revisions

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{{Seed}}
[[Image:2fpp.png|left|200px]]


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==Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions==
The line below this paragraph, containing "STRUCTURE_2fpp", creates the "Structure Box" on the page.
<StructureSection load='2fpp' size='340' side='right'caption='[[2fpp]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2fpp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FPP FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NEP:N1-PHOSPHONOHISTIDINE'>NEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_2fpp|  PDB=2fpp  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fpp OCA], [https://pdbe.org/2fpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fpp RCSB], [https://www.ebi.ac.uk/pdbsum/2fpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fpp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUCB2_PIG SUCB2_PIG] Catalyzes the GTP-dependent ligation of succinate and CoA to form succinyl-CoA (By similarity).
== 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/fp/2fpp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2fpp ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two isoforms of succinyl-CoA synthetase exist in mammals, one specific for ATP and the other for GTP. The GTP-specific form of pig succinyl-CoA synthetase has been crystallized in the presence of GTP and the structure determined to 2.1 A resolution. GTP is bound in the ATP-grasp domain, where interactions of the guanine base with a glutamine residue (Gln-20beta) and with backbone atoms provide the specificity. The gamma-phosphate interacts with the side chain of an arginine residue (Arg-54beta) and with backbone amide nitrogen atoms, leading to tight interactions between the gamma-phosphate and the protein. This contrasts with the structures of ATP bound to other members of the family of ATP-grasp proteins where the gamma-phosphate is exposed, free to react with the other substrate. To test if GDP would interact with GTP-specific succinyl-CoA synthetase in the same way that ADP interacts with other members of the family of ATP-grasp proteins, the structure of GDP bound to GTP-specific succinyl-CoA synthetase was also determined. A comparison of the conformations of GTP and GDP shows that the bases adopt the same position but that changes in conformation of the ribose moieties and the alpha- and beta-phosphates allow the gamma-phosphate to interact with the arginine residue and amide nitrogen atoms in GTP, while the beta-phosphate interacts with these residues in GDP. The complex of GTP with succinyl-CoA synthetase shows that the enzyme is able to protect GTP from hydrolysis when the active-site histidine residue is not in position to be phosphorylated.


===Crystal structure of pig GTP-specific succinyl-CoA synthetase from polyethylene glycol with chloride ions===
Interactions of GTP with the ATP-grasp domain of GTP-specific succinyl-CoA synthetase.,Fraser ME, Hayakawa K, Hume MS, Ryan DG, Brownie ER J Biol Chem. 2006 Apr 21;281(16):11058-65. Epub 2006 Feb 15. PMID:16481318<ref>PMID:16481318</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2fpp" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_16481318}}, adds the Publication Abstract to the page
*[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 16481318 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_16481318}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2FPP is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FPP OCA].
 
==Reference==
<ref group="xtra">PMID:16481318</ref><references group="xtra"/>
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Brownie, E R.]]
[[Category: Brownie ER]]
[[Category: Fraser, M E.]]
[[Category: Fraser ME]]
[[Category: Hayakawa, K.]]
[[Category: Hayakawa K]]
[[Category: Hume, M S.]]
[[Category: Hume MS]]
[[Category: Ryan, D G.]]
[[Category: Ryan DG]]
[[Category: Active site phosphohistidine residue]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:12:49 2009''
Retrieved from "https://proteopedia.org/2fpp"