1agy
From Proteopedia
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| - | [[Image:1agy.gif|left|200px]] | + | [[Image:1agy.gif|left|200px]] |
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| - | '''THE 1.15 ANGSTROM REFINED STRUCTURE OF FUSARIUM SOLANI PISI CUTINASE''' | + | {{Structure |
| + | |PDB= 1agy |SIZE=350|CAPTION= <scene name='initialview01'>1agy</scene>, resolution 1.15Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE 1.15 ANGSTROM REFINED STRUCTURE OF FUSARIUM SOLANI PISI CUTINASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AGY is a [ | + | 1AGY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_solani_subsp._pisi Fusarium solani subsp. pisi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGY OCA]. |
==Reference== | ==Reference== | ||
| - | Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis., Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C, J Mol Biol. 1997 May 16;268(4):779-99. PMID:[http:// | + | Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis., Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C, J Mol Biol. 1997 May 16;268(4):779-99. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9175860 9175860] |
[[Category: Fusarium solani subsp. pisi]] | [[Category: Fusarium solani subsp. pisi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine esterase]] | [[Category: serine esterase]] | ||
| - | ''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 09:57:25 2008'' |
Revision as of 07:57, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE 1.15 ANGSTROM REFINED STRUCTURE OF FUSARIUM SOLANI PISI CUTINASE
Overview
X-ray data have been recorded to 1.0 A resolution from a crystal of Fusarium solani cutinase using synchrotron radiation and an imaging-plate scanner. The anisotropic treatment of thermal motion led to a fivefold increase in accuracy and to a considerable quality improvement in the electron density maps with respect to an intermediate isotropic model. The final model has an R-factor of 9.4%, with a mean coordinate error of 0.021 A, as estimated from inversion of the least-squares matrix. The availability of an accurate structure at atomic resolution and of meaningful estimates of the errors in its atomic parameters, allowed an extensive analysis of several stereochemical parameters, such as peptide planarity, main-chain and some side-chain bond distances. The hydrogen atoms could be clearly identified in the electron density, thus providing unambiguous evidence on the protonation state of the catalytic histidine residue. The atomic resolution revealed an appreciable extent of flexibility in the cutinase active site, which might be correlated with a possible adaptation to different substrates. The anisotropic treatment of thermal factors provided insights into the anisotropic nature of motions. The analysis of these motions in the two loops delimiting the catalytic crevice pointed out a "breath-like" movement in the substrate binding region of cutinase.
About this Structure
1AGY is a Single protein structure of sequence from Fusarium solani subsp. pisi. Full crystallographic information is available from OCA.
Reference
Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis., Longhi S, Czjzek M, Lamzin V, Nicolas A, Cambillau C, J Mol Biol. 1997 May 16;268(4):779-99. PMID:9175860
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