2a9j: Difference between revisions

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[[Image:2a9j.png|left|200px]]


{{STRUCTURE_2a9j|  PDB=2a9j  |  SCENE=  }}
==Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)==
 
<StructureSection load='2a9j' size='340' side='right'caption='[[2a9j]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
===Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2a9j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A9J FirstGlance]. <br>
{{ABSTRACT_PUBMED_17052986}}
</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=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a9j OCA], [https://pdbe.org/2a9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a9j RCSB], [https://www.ebi.ac.uk/pdbsum/2a9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a9j ProSAT]</span></td></tr>
[[2a9j]] is a 2 chain structure of [[Bisphosphoglycerate mutase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A9J OCA].  
</table>
== Disease ==
[https://www.uniprot.org/uniprot/PMGE_HUMAN PMGE_HUMAN] Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:[https://omim.org/entry/222800 222800]. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.<ref>PMID:2542247</ref> <ref>PMID:1421379</ref> <ref>PMID:15054810</ref>
== Function ==
[https://www.uniprot.org/uniprot/PMGE_HUMAN PMGE_HUMAN] Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.
== 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/a9/2a9j_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=2a9j ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Bisphosphoglycerate mutase|Bisphosphoglycerate mutase]]
*[[Phosphoglycerate mutase 3D structures|Phosphoglycerate mutase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:017052986</ref><references group="xtra"/>
__TOC__
[[Category: Bisphosphoglycerate mutase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Gong, W.]]
[[Category: Large Structures]]
[[Category: Wang, Y.]]
[[Category: Gong W]]
[[Category: 3-phosphoglycerate]]
[[Category: Wang Y]]
[[Category: Bisphosphoglycerate mutase]]
[[Category: Isomerase]]

Latest revision as of 16:40, 13 March 2024

Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)Human bisphosphoglycerate mutase complexed with 3-phosphoglycerate (17 days)

Structural highlights

2a9j is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PMGE_HUMAN Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.[1] [2] [3]

Function

PMGE_HUMAN Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.

Evolutionary Conservation

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

See Also

References

  1. Rosa R, Blouquit Y, Calvin MC, Prome D, Prome JC, Rosa J. Isolation, characterization, and structure of a mutant 89 Arg----Cys bisphosphoglycerate mutase. Implication of the active site in the mutation. J Biol Chem. 1989 May 15;264(14):7837-43. PMID:2542247
  2. Lemarchandel V, Joulin V, Valentin C, Rosa R, Galacteros F, Rosa J, Cohen-Solal M. Compound heterozygosity in a complete erythrocyte bisphosphoglycerate mutase deficiency. Blood. 1992 Nov 15;80(10):2643-9. PMID:1421379
  3. Hoyer JD, Allen SL, Beutler E, Kubik K, West C, Fairbanks VF. Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. Am J Hematol. 2004 Apr;75(4):205-8. PMID:15054810 doi:10.1002/ajh.20014

2a9j, resolution 2.00Å

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