3k4q
From Proteopedia
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k4/3k4q_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k4/3k4q_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 09:24, 26 December 2018
Aspergillus niger Phytase in complex with myo-inositol hexakis sulfate
<StructureSection load='3k4q' size='340' side='right' caption='3k4q, resolution 2.20Å' scene=>
Structural highlights
| 3k4q is a 2 chain structure with sequence from A. niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. | |
| Ligands: | <scene name='pdbligand=IHS:D-MYO-INOSITOL-HEXASULPHATE'>IHS</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
| Related: | 1ihp, 2gfi, 1dkl, 1dkq, 1qfx, 3k4p |
| Gene: | PhyA (A. niger) |
| Activity: | 3-phytase, with EC number 3.1.3.8 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[PHYA_ASPNG] Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Phytases hydrolyse the phosphomonoesters of phytate (myo-inositol-1,2,3,4,5,6-hexakis phosphate) and thus find uses in plant and animal production through the mobilisation of phosphorus from this source. The structure of partially deglycosylated Aspergillus niger PhyA is presented in apo form and in complex with the potent inhibitor myo-inositol-1,2,3,4,5,6-hexakis sulfate, which by analogy with phytate provides a snapshot of the Michaelis complex. The structure explains the enzyme's preference for the 3'-phosphate of phytate. The apo-and inhibitor-bound forms are similar and no induced-fit mechanism operates. Furthermore the enzyme structure is apparently unaffected by the presence of glycosides on the surface. The new structures of A. niger PhyA are discussed in the context of protein engineering studies aimed at modulating pH preference and stability.
The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic.,Oakley AJ Biochem Biophys Res Commun. 2010 Jul 9;397(4):745-9. Epub 2010 Jun 10. PMID:20541524[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Oakley AJ. The structure of Aspergillus niger phytase PhyA in complex with a phytate mimetic. Biochem Biophys Res Commun. 2010 Jul 9;397(4):745-9. Epub 2010 Jun 10. PMID:20541524 doi:10.1016/j.bbrc.2010.06.024
Contents |
</StructureSection>
