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| | {{STRUCTURE_1lys| PDB=1lys | SCENE= }} | | {{STRUCTURE_1lys| PDB=1lys | SCENE= }} |
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| - | '''X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES'''
| + | ===X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES=== |
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| - | ==Overview==
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| - | A monoclinic crystal of hen egg lysozyme (HEL, E.C. 3.2.1.17) was obtained at 313 K from a 10%(w/v) NaCl solution at pH 7.6 containing 5%(v/v) 1-propanol. Cell dimensions were a = 27.23, b = 63.66, c = 59.12 A and beta = 92.9 degrees, and the space group was P2(1). The unit cell contains four molecules (V(m) = 1.79 A(3) Da(-1)). The structure was solved by the isomorphous replacement method with anomalous scattering followed by phase improvement by the solvent-flattening method. The refinement of the structure was carried out by the simulated-annealing method. The conventional R value was 0.187 for 18 260 reflections [|F(o)| > 3sigma(F)] in the resolution range 10-1.72 A. The r.m.s. deviations from the ideal bond distances and angles were 0.015 A and 3.0 degrees, respectively. The two molecules in the asymmetric unit are related by a translation of half a lattice unit along the a and c axes. The r.m.s. difference of equivalent C(alpha) atoms between the two molecules was 0.64 A and the largest difference was 3.57 A for Gly71. A significant structural change was observed in the regions of residues 45-50, 65-73 and 100-104. The residues 45-50, which connect two beta-strands, are shifted parallel to the beta-sheet plane between the two molecules. The residues 100-104 belong to the substrate-binding site (subsite A) and the high flexibility of this region may be responsible for the binding of the substrate and the release of reaction products.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15299435}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15299435 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15299435}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Single protein]] | | [[Category: Single protein]] |
| | [[Category: Harata, K.]] | | [[Category: Harata, K.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:25:57 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:50:33 2008'' |
Revision as of 19:50, 2 July 2008
Template:STRUCTURE 1lys
X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES
Template:ABSTRACT PUBMED 15299435
About this Structure
1LYS is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313 K. Comparison of two independent molecules., Harata K, Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):250-7. PMID:15299435
Page seeded by OCA on Wed Jul 2 22:50:33 2008
