View source for 3nvl


==Crystal Structure of Phosphoglycerate Mutase from Trypanosoma brucei==
<StructureSection load='3nvl' size='340' side='right'caption='[[3nvl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3nvl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei_TREU927 Trypanosoma brucei brucei TREU927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NVL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NVL 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3nvl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nvl OCA], [https://pdbe.org/3nvl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nvl RCSB], [https://www.ebi.ac.uk/pdbsum/3nvl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nvl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q38AH1_TRYB2 Q38AH1_TRYB2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phosphoglycerate mutases (PGAMs) participate in both the glycolytic and the gluconeogenic pathways in reversible isomerization of 3-phosphoglycerate and 2-phosphoglycerate. PGAMs are members of two distinct protein families: enzymes that are dependent on or independent of the 2,3-bisphosphoglycerate cofactor. We determined the X-ray structure of the monomeric Trypanosoma brucei independent PGAM (TbiPGAM) in its apoenzyme form, and confirmed this observation by small angle X-ray scattering data. Comparing the TbiPGAM structure with the Leishmania mexicana independent PGAM structure, previously reported with a phosphoglycerate molecule bound to the active site, revealed the domain movement resulting from active site occupation. The structure reported here shows the interaction between Asp319 and the metal bound to the active site, and its contribution to the domain movement. Substitution of the metal-binding residue Asp319 by Ala resulted in complete loss of independent PGAM activity, and showed for the first time its involvement in the enzyme's function. As TbiPGAM is an attractive molecular target for drug development, the apoenzyme conformation described here provides opportunities for its use in structure-based drug design approaches. Database Structural data for the Trypanosoma brucei 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM) has been deposited with the Research Collaboratory for Structural Bioinformatics (RCSB) Protein Data Bank under code 3NVL. Structured digital abstract * TbiPGAM and TbiPGAM bind by x-raycrystallography (View interaction).

Structural role of the active-site metal in the conformation of Trypanosoma brucei phosphoglycerate mutase.,Mercaldi GF, Pereira HM, Cordeiro AT, Michels PA, Thiemann OH FEBS J. 2012 Jun;279(11):2012-21. doi: 10.1111/j.1742-4658.2012.08586.x. Epub, 2012 Apr 24. PMID:22458781<ref>PMID:22458781</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3nvl" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trypanosoma brucei brucei TREU927]]
[[Category: Andricopulo AD]]
[[Category: Cordeiro AT]]
[[Category: Mercaldi GF]]
[[Category: Pereira HM]]
[[Category: Thiemann OH]]