1skb: Difference between revisions
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[[Image:1skb.gif|left|200px]] | [[Image:1skb.gif|left|200px]] | ||
'''Crystallographic snapshots of Aspergillus fumigatus phytase revealing its enzymatic dynamics''' | {{Structure | ||
|PDB= 1skb |SIZE=350|CAPTION= <scene name='initialview01'>1skb</scene>, resolution 1.58Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8] | |||
|GENE= PHYA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5085 Aspergillus fumigatus]) | |||
}} | |||
'''Crystallographic snapshots of Aspergillus fumigatus phytase revealing its enzymatic dynamics''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SKB is a [ | 1SKB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SKB OCA]. | ||
==Reference== | ==Reference== | ||
Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics., Liu Q, Huang Q, Lei XG, Hao Q, Structure. 2004 Sep;12(9):1575-83. PMID:[http:// | Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics., Liu Q, Huang Q, Lei XG, Hao Q, Structure. 2004 Sep;12(9):1575-83. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15341723 15341723] | ||
[[Category: 3-phytase]] | [[Category: 3-phytase]] | ||
[[Category: Aspergillus fumigatus]] | [[Category: Aspergillus fumigatus]] | ||
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[[Category: NDG]] | [[Category: NDG]] | ||
[[Category: big alpha/beta domain]] | [[Category: big alpha/beta domain]] | ||
[[Category: catalytic | [[Category: catalytic dynamic]] | ||
[[Category: catalytic | [[Category: catalytic site]] | ||
[[Category: product release pathway]] | [[Category: product release pathway]] | ||
[[Category: small alpha domain]] | [[Category: small alpha domain]] | ||
[[Category: water | [[Category: water structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:06:05 2008'' |
Revision as of 15:06, 20 March 2008
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, resolution 1.58Å | |||||||
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Ligands: | and | ||||||
Gene: | PHYA (Aspergillus fumigatus) | ||||||
Activity: | 3-phytase, with EC number 3.1.3.8 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystallographic snapshots of Aspergillus fumigatus phytase revealing its enzymatic dynamics
OverviewOverview
Understanding of the atomic movements involved in an enzymatic reaction needs structural information on the active and inactive native enzyme molecules and on the enzyme-substrate, enzyme-intermediate, and enzyme-product(s) complexes. By using the X-ray crystallographic method, four crystal structures of Aspergillus fumigatus phytase were obtained at resolution higher than 1.7 A. The pH-dependent catalytic activity of A. fumigatus phytase was linked to three water molecules that may prevent the substrate from binding and thus block nucleophilic attack of the catalytic imidazole nitrogen. Comparison of various structures also identified the water molecule that attacks the phosphamide bond during the hydrolysis process, and established the hydrolysis pathway of the intermediate. Additionally, two reaction product phosphates were observed at the active site, suggesting a possible product release pathway after hydrolysis of the intermediate. These results can help explain the catalytic mechanism throughout the whole acid phosphatase family, as all key residues are conserved.
About this StructureAbout this Structure
1SKB is a Single protein structure of sequence from Aspergillus fumigatus. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics., Liu Q, Huang Q, Lei XG, Hao Q, Structure. 2004 Sep;12(9):1575-83. PMID:15341723
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