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3hde
From Proteopedia
(Difference between revisions)
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| - | {{Seed}} | ||
| - | [[Image:3hde.png|left|200px]] | ||
| - | < | + | ==Crystal structure of full-length endolysin R21 from phage 21== |
| - | + | <StructureSection load='3hde' size='340' side='right'caption='[[3hde]], [[Resolution|resolution]] 1.95Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3hde]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp21 Bpp21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HDE FirstGlance]. <br> | |
| - | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hdf|3hdf]]</div></td></tr> | |
| - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">R ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10711 BPP21])</td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=3hde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hde OCA], [https://pdbe.org/3hde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hde RCSB], [https://www.ebi.ac.uk/pdbsum/3hde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hde ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/LYS_BPP21 LYS_BPP21]] Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Acts as a transglycosylase. | ||
| + | == 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/hd/3hde_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/main_output.php?pdb_ID=3hde ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | R(21), the lysozyme of coliphage 21, has an N-terminal signal-anchor-release (SAR) domain that directs its secretion in a membrane-tethered, inactive form and then its release and activation in the periplasm. Both genetic and crystallographic studies show that the SAR domain, once extracted from the bilayer, refolds into the body of the enzyme and effects muralytic activation by repositioning one residue of the canonical lysozyme catalytic triad. | ||
| - | + | Regulation of a muralytic enzyme by dynamic membrane topology.,Sun Q, Kuty GF, Arockiasamy A, Xu M, Young R, Sacchettini JC Nat Struct Mol Biol. 2009 Nov;16(11):1192-4. Epub 2009 Nov 1. PMID:19881499<ref>PMID:19881499</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3hde" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Bpp21]] |
| - | + | [[Category: Large Structures]] | |
| - | + | ||
| - | == | + | |
| - | < | + | |
| - | [[Category: | + | |
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
| - | [[Category: Arockiasamy, A | + | [[Category: Arockiasamy, A]] |
| - | [[Category: Caronna, E | + | [[Category: Caronna, E]] |
| - | [[Category: McKee, E | + | [[Category: McKee, E]] |
| - | [[Category: Sacchettini, J C | + | [[Category: Sacchettini, J C]] |
| - | [[Category: Sun, Q | + | [[Category: Sun, Q]] |
[[Category: Antimicrobial]] | [[Category: Antimicrobial]] | ||
[[Category: Bacteriolytic enzyme]] | [[Category: Bacteriolytic enzyme]] | ||
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[[Category: Late protein]] | [[Category: Late protein]] | ||
[[Category: Lysozyme-like]] | [[Category: Lysozyme-like]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 20 16:33:16 2010'' | ||
Current revision
Crystal structure of full-length endolysin R21 from phage 21
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