3gp3: Difference between revisions

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<StructureSection load='3gp3' size='340' side='right'caption='[[3gp3]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='3gp3' size='340' side='right'caption='[[3gp3]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3gp3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pseudomallei"_whitmore_1913 "bacillus pseudomallei" whitmore 1913]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GP3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3gp3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GP3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ezn|3ezn]], [[3fdz|3fdz]], [[3gp5|3gp5]], [[3gw8|3gw8]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PO3:PHOSPHITE+ION'>PO3</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gpmA, BPSL0443 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=28450 "Bacillus pseudomallei" Whitmore 1913])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] </span></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=3gp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gp3 OCA], [https://pdbe.org/3gp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gp3 RCSB], [https://www.ebi.ac.uk/pdbsum/3gp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gp3 ProSAT]</span></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=3gp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gp3 OCA], [https://pdbe.org/3gp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gp3 RCSB], [https://www.ebi.ac.uk/pdbsum/3gp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gp3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GPMA_BURPS GPMA_BURPS]] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).  
[https://www.uniprot.org/uniprot/GPMA_BURP1 GPMA_BURP1] Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).[HAMAP-Rule:MF_01039]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=3gp3 ConSurf].
</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=3gp3 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Burkholderia pseudomallei is a soil-dwelling bacterium endemic to Southeast Asia and Northern Australia. Burkholderia is responsible for melioidosis, a serious infection of the skin. The enzyme 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (PGAM) catalyzes the interconversion of 3-phosphoglycerate and 2-phosphoglycerate, a key step in the glycolytic pathway. As such it is an extensively studied enzyme and X-ray crystal structures of PGAM enzymes from multiple species have been elucidated. Vanadate is a phosphate mimic that is a powerful tool for studying enzymatic mechanisms in phosphoryl-transfer enzymes such as phosphoglycerate mutase. However, to date no X-ray crystal structures of phosphoglycerate mutase have been solved with vanadate acting as a substrate mimic. Here, two vanadate complexes together with an ensemble of substrate and fragment-bound structures that provide a comprehensive picture of the function of the Burkholderia enzyme are reported.
An ensemble of structures of Burkholderia pseudomallei 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase.,Davies DR, Staker BL, Abendroth JA, Edwards TE, Hartley R, Leonard J, Kim H, Rychel AL, Hewitt SN, Myler PJ, Stewart LJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1044-50. Epub 2011 Aug 13. PMID:21904048<ref>PMID:21904048</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3gp3" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus pseudomallei whitmore 1913]]
[[Category: Burkholderia pseudomallei]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Phosphoglycerate mutase]]
[[Category: Structural genomic]]
[[Category: Decode]]
[[Category: Glycolysis]]
[[Category: Isomerase]]
[[Category: Niaid]]
[[Category: Phosphoglyceromutase]]
[[Category: Sbri]]
[[Category: Ssgcid]]
[[Category: Uwppg]]

Latest revision as of 12:55, 21 February 2024

Crystal structure of phosphoglyceromutase from Burkholderia pseudomallei with 2-phosphoserineCrystal structure of phosphoglyceromutase from Burkholderia pseudomallei with 2-phosphoserine

Structural highlights

3gp3 is a 4 chain structure with sequence from Burkholderia pseudomallei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GPMA_BURP1 Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate (By similarity).[HAMAP-Rule:MF_01039]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3gp3, resolution 1.50Å

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