135l
From Proteopedia
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- | [[ | + | ==X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION== |
+ | <StructureSection load='135l' size='340' side='right' caption='[[135l]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[135l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=135L FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=135l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=135l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=135l RCSB], [http://www.ebi.ac.uk/pdbsum/135l PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/35/135l_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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<ref>PMID:15299509</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
- | *[[ | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Meleagris gallopavo]] | [[Category: Meleagris gallopavo]] | ||
[[Category: Harata, K.]] | [[Category: Harata, K.]] |
Revision as of 08:29, 23 July 2014
X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION
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