2d6b: Difference between revisions
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<StructureSection load='2d6b' size='340' side='right'caption='[[2d6b]], [[Resolution|resolution]] 1.25Å' scene=''> | <StructureSection load='2d6b' size='340' side='right'caption='[[2d6b]], [[Resolution|resolution]] 1.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2d6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2d6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D6B FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.25Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=202:BROMIC+ACID'>202</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d6b OCA], [https://pdbe.org/2d6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d6b RCSB], [https://www.ebi.ac.uk/pdbsum/2d6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d6b ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2d6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d6b OCA], [https://pdbe.org/2d6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d6b RCSB], [https://www.ebi.ac.uk/pdbsum/2d6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d6b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] 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. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mesters JR]] | |||
[[Category: Mesters | [[Category: Ondracek J]] | ||
[[Category: Ondracek | |||
Latest revision as of 10:38, 23 August 2023
Novel Bromate Species trapped within a Protein CrystalNovel Bromate Species trapped within a Protein Crystal
Structural highlights
FunctionLYSC_CHICK 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. Has bacteriolytic activity against M.luteus.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedOnly a few protein-oxoanion crystal complexes have been described to date. Here, the structure of a protein soaked in a bromate solution has been determined to a resolution of 1.25 A and refined to final overall R/R(free) values of 18.04/21.3 (isotropic) and 11.25/14.67 (anisotropic). In contrast to the single-model approach, refinement of an ensemble of ten models enabled us to determine variances and statistically evaluate bond-length distances and angles in the oxoanions. In total, nine bromate positions, including two BrO(3)(-) x HBrO(3) dimer species, have been identified on the basis of the anomalous signal of the Br atoms. For all bromate ions, the main-chain amide atoms of the protein were identified as the dominant binding positions, a useful property in any experimental phase-determination experiment. An ensemble of crystallographic models enables the description of novel bromate-oxoanion species trapped within a protein crystal.,Ondracek J, Mesters JR Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):996-1001. Epub 2006, Aug 19. PMID:16929100[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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