1agy: Difference between revisions

Revision as of 16:49, 30 June 2008

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File:1agy.png

Template:STRUCTURE 1agy

THE 1.15 ANGSTROM REFINED STRUCTURE OF FUSARIUM SOLANI PISI CUTINASETHE 1.15 ANGSTROM REFINED STRUCTURE OF FUSARIUM SOLANI PISI CUTINASE

Template:ABSTRACT PUBMED 9175860

About this StructureAbout this Structure

1AGY is a Single protein structure of sequence from Fusarium solani subsp. pisi. Full crystallographic information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1agy.gif|left|200px]]
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-'''THE 1.15 ANGSTROM REFINED STRUCTURE OF FUSARIUM SOLANI PISI CUTINASE'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9175860}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9175860}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Serine esterase]]
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