1llh
From Proteopedia
(Difference between revisions)
| (9 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_1llh| PDB=1llh | SCENE= }} | ||
| - | ===ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY TERTIARY STRUCTURE CONTACTS=== | ||
| - | {{ABSTRACT_PUBMED_11847274}} | ||
| - | == | + | ==ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY TERTIARY STRUCTURE CONTACTS== |
| - | [[http://www.uniprot.org/uniprot/ | + | <StructureSection load='1llh' size='340' side='right'caption='[[1llh]], [[Resolution|resolution]] 1.80Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1llh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1joz 1joz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=1llh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llh OCA], [https://pdbe.org/1llh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1llh RCSB], [https://www.ebi.ac.uk/pdbsum/1llh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llh ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref> | ||
| + | == 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/ll/1llh_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=1llh ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | alpha-helices within proteins are often terminated (capped) by distinctive configurations of the polypeptide chain. Two common arrangements are the Schellman motif and the alternative alpha(L) motif. Rose and coworkers developed stereochemical rules to identify the locations of such motifs in proteins of unknown structure based only on their amino acid sequences. To check the effectiveness of these rules, they made specific predictions regarding the structural and thermodynamic consequences of certain mutations in T4 lysozyme. We have constructed these mutants and show here that they have neither the structure nor the stability that was predicted. The results show the complexity of the protein-folding problem. Comparison of known protein structures may show that a characteristic sequence of amino acids (a sequence motif) corresponds to a conserved structural motif. In any particular protein, however, changes in other parts of the sequence may result in a different conformation. The structure is determined by sequence as a whole, not by parts considered in isolation. | ||
| - | + | A test of proposed rules for helix capping: implications for protein design.,Sagermann M, Martensson LG, Baase WA, Matthews BW Protein Sci. 2002 Mar;11(3):516-21. PMID:11847274<ref>PMID:11847274</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | < | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 1llh" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: Baase | + | ==See Also== |
| - | [[Category: Martensson | + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] |
| - | [[Category: Matthews | + | == References == |
| - | [[Category: Sagermann | + | <references/> |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Escherichia virus T4]] | |
| - | + | [[Category: Large Structures]] | |
| + | [[Category: Baase WA]] | ||
| + | [[Category: Martensson L-G]] | ||
| + | [[Category: Matthews BW]] | ||
| + | [[Category: Sagermann M]] | ||
Current revision
ARE CARBOXY TERMINII OF HELICES CODED BY THE LOCAL SEQUENCE OR BY TERTIARY STRUCTURE CONTACTS
| |||||||||||
