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1hhl

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(New page: 200px<br /> <applet load="1hhl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hhl, resolution 1.9&Aring;" /> '''THE THREE-DIMENSIONA...)
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[[Image:1hhl.gif|left|200px]]<br />
 
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<applet load="1hhl" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hhl, resolution 1.9&Aring;" />
 
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'''THE THREE-DIMENSIONAL STRUCTURE OF PHEASANT AND GUINEA-FOWL EGG LYSOZYMES'''<br />
 
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==Overview==
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==THE THREE-DIMENSIONAL STRUCTURE OF PHEASANT AND GUINEA-FOWL EGG LYSOZYMES==
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The crystal structures of pheasant and guinea fowl lysozymes have been, determined by X-ray diffraction methods. Guinea fowl lysozyme crystallizes, in space group P6(1)22 with cell dimensions a = 89.2 A and c = 61.7 A. The, structure was refined to a final crystallographic R-factor of 17.0% for, 8,854 observed reflections in the resolution range 6-1.9 A. Crystals of, pheasant lysozyme are tetragonal, space group P4(3)2(1)2, with a = 98.9 A, c = 69.3 A and 2 molecules in the asymmetric unit. The final R-factor is, 17.8% to 2.1 A resolution. The RMS deviation from ideality is 0.010 A for, bond lengths and 2.5 degrees for bond angles in both models. Three amino, acid positions beneath the active site are occupied by Thr 40, Ile 55, and, Ser 91 in hen, pheasant, and other avian lysozymes, and by Ser 40, Val 55, and Thr 91 in guinea fowl and American quail lysozymes. In spite of their, internal location, the structural changes associated with these, substitutions are small. The pheasant enzyme has an additional N-terminal, glycine residue, probably resulting from an evolutionary shift in the site, of cleavage of prelysozyme. In the 3-dimensional structure, this amino, acid partially fills a cleft on the surface of the molecule, close to the, C alpha atom of Gly 41 and absent in lysozymes from other species (which, have a large side-chain residue at position 41: Gln, His, Arg, or Lys)., The overall structures are similar to those of other c-type lysozymes, with the largest deviations occurring in surface loops. Comparison of the, unliganded and antibody-bound models of pheasant lysozyme suggests that, surface complementarity of contacting surfaces in the antigen-antibody, complex is the result of local, small rearrangements in the epitope., Structural evidence based upon this and other complexes supports the, notion that antigenic variation in c-type lysozymes is primarily the, result of amino acid substitutions, not of gross structural changes.
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<StructureSection load='1hhl' size='340' side='right'caption='[[1hhl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1hhl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Numida_meleagris Numida meleagris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HHL FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hhl OCA], [https://pdbe.org/1hhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hhl RCSB], [https://www.ebi.ac.uk/pdbsum/1hhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hhl ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_NUMME LYSC_NUMME] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/1hhl_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=1hhl ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1HHL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Numida_meleagris Numida meleagris]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HHL OCA].
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structures of pheasant and guinea fowl egg-white lysozymes., Lescar J, Souchon H, Alzari PM, Protein Sci. 1994 May;3(5):788-98. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8061608 8061608]
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[[Category: Large Structures]]
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[[Category: Lysozyme]]
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[[Category: Numida meleagris]]
[[Category: Numida meleagris]]
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[[Category: Single protein]]
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[[Category: Alzari PM]]
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[[Category: Alzari, P.M.]]
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[[Category: Lescar J]]
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[[Category: Lescar, J.]]
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[[Category: hydrolase(o-glycosyl)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:32:01 2007''
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THE THREE-DIMENSIONAL STRUCTURE OF PHEASANT AND GUINEA-FOWL EGG LYSOZYMES

PDB ID 1hhl

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