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Phosphomannomutase

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== Structural highlights ==
== Structural highlights ==
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The PMM structure contains a <scene name='48/481638/Cv/2'>core domain and a cap domain</scene>. It is known that in order for the substrate to bind, the cap must dissociate from the core domain and then re-associate to seal the active site from solvent molecules. The <scene name='48/481638/Cv/4'>active site of PMM is located at the interface of the core and cap domains of the molecule</scene><ref>PMID:16540464</ref>. Water molecules shown as red spheres.
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The PMM structure contains a <scene name='48/481638/Cv/6'>core domain and a cap domain</scene>. It is known that in order for the substrate to bind, the cap must dissociate from the core domain and then re-associate to seal the active site from solvent molecules. The <scene name='48/481638/Cv/4'>active site of PMM is located at the interface of the core and cap domains of the molecule</scene><ref>PMID:16540464</ref>. Water molecules shown as red spheres.
</StructureSection>
</StructureSection>

Revision as of 09:40, 4 September 2016

Human phosphomannomutase 1 complex with α-D-mannose-1-phosphate and Mg+2 ion (green) (PDB entry 2fue)

Drag the structure with the mouse to rotate

3D Structures of phosphomannomutase

Updated on 04-September-2016

References

  1. ↑ Matthijs G, Schollen E, Pardon E, Veiga-Da-Cunha M, Jaeken J, Cassiman JJ, Van Schaftingen E. Mutations in PMM2, a phosphomannomutase gene on chromosome 16p13, in carbohydrate-deficient glycoprotein type I syndrome (Jaeken syndrome). Nat Genet. 1997 May;16(1):88-92. PMID:9140401 doi:10.1038/ng0597-88
  2. ↑ Silvaggi NR, Zhang C, Lu Z, Dai J, Dunaway-Mariano D, Allen KN. The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal the structural basis of congenital disorder of glycosylation type 1a. J Biol Chem. 2006 May 26;281(21):14918-26. Epub 2006 Mar 15. PMID:16540464 doi:http://dx.doi.org/10.1074/jbc.M601505200

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