135l
From Proteopedia
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[[Image:135l.gif|left|200px]] | [[Image:135l.gif|left|200px]] | ||
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| - | | | + | {{STRUCTURE_135l| PDB=135l | SCENE= }} |
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'''X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION''' | '''X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 135L is a [[Single protein]] structure | + | 135L is a [[Single protein]] structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1lz3 1lz3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=135L OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Harata, K.]] | [[Category: Harata, K.]] | ||
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Revision as of 06:29, 2 May 2008
X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION
Overview
Monoclinic crystals of turkey egg lysozyme (TEL, E.C. 3.2.1.17) were obtained from 2.2 M ammonium sulfate solution at pH 4.2. They belong to space group P2(1) with unit-cell dimensions a = 38.07, b = 33.20, c = 46.12 A and beta = 110.1 degrees, and contain one molecule in the asymmetric unit (V(m) = 1.91 A(3) Da(-1)). The three-dimensional structure of TEL was solved by the method of multiple isomorphous replacement with anomalous scattering. Area detector data to 1.5 A resolution from native and heavy-atom derivatives were used for the structure determination. The structure was refined by the simulated-annealing method with diffraction data of 10-1.30 A resolution. The conventional R factor was 0.189. The root-mean-square deviations from ideal bond distances and angles were 0.016 A and 2.9 degrees, respectively. The backbone structure of TEL is very similar to that of hen egg lysozyme (HEL) and the difference in seven amino-acid residues does not affect the basic folding of the polypeptide chain. Except for the region from Gly101 to Gly104, the geometry of the active-site cleft is conserved between TEL and HEL. The Gly101 residue is located at the end of the sugar-binding site and the structural change in this region between TEL and HEL is considered to be responsible for the difference in their enzymatic properties.
About this Structure
135L is a Single protein structure. This structure supersedes the now removed PDB entry 1lz3. Full crystallographic information is available from OCA.
Reference
X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution., Harata K, Acta Crystallogr D Biol Crystallogr. 1993 Sep 1;49(Pt 5):497-504. PMID:15299509 Page seeded by OCA on Fri May 2 09:29:17 2008
