1cv6: Difference between revisions
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<StructureSection load='1cv6' size='340' side='right' caption='[[1cv6]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1cv6' size='340' side='right' caption='[[1cv6]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cv6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CV6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1cv6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CV6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HED:2-HYDROXYETHYL+DISULFIDE'>HED</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ctw|1ctw]], [[1cu0|1cu0]], [[1cu2|1cu2]], [[1cu3|1cu3]], [[1cu6|1cu6]], [[1cu5|1cu5]], [[1cup|1cup]], [[1cuq|1cuq]], [[1cv0|1cv0]], [[1cv1|1cv1]], [[1qsq|1qsq]], [[1cv4|1cv4]], [[1cv3|1cv3]], [[1cv5|1cv5]], [[1cvk|1cvk]], [[1d2w|1d2w]], [[1d2y|1d2y]], [[1d3f|1d3f]], [[1d3j|1d3j]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ctw|1ctw]], [[1cu0|1cu0]], [[1cu2|1cu2]], [[1cu3|1cu3]], [[1cu6|1cu6]], [[1cu5|1cu5]], [[1cup|1cup]], [[1cuq|1cuq]], [[1cv0|1cv0]], [[1cv1|1cv1]], [[1qsq|1qsq]], [[1cv4|1cv4]], [[1cv3|1cv3]], [[1cv5|1cv5]], [[1cvk|1cvk]], [[1d2w|1d2w]], [[1d2y|1d2y]], [[1d3f|1d3f]], [[1d3j|1d3j]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GENE E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</td></tr> | |||
<tr id='activity'><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 id='activity'><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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cv6 OCA], [http://pdbe.org/1cv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cv6 RCSB], [http://www.ebi.ac.uk/pdbsum/1cv6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cv6 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cv6 OCA], [http://pdbe.org/1cv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cv6 RCSB], [http://www.ebi.ac.uk/pdbsum/1cv6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cv6 ProSAT]</span></td></tr> | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/1cv6_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cv/1cv6_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1cv6" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1cv6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bpt4]] | |||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Baase, W A]] | [[Category: Baase, W A]] | ||
Revision as of 09:08, 31 January 2018
T4 LYSOZYME MUTANT V149MT4 LYSOZYME MUTANT V149M
Structural highlights
Function[LYS_BPT4] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan. 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 PubMedIn an attempt to identify a systematic relation between the structure of a protein and its folding kinetics, the rate of folding was determined for 20 mutants of T4 lysozyme in which a bulky, buried, nonpolar wild-type residue (Leu, Ile, Phe, Val, or Met) was substituted with alanine. Methionine, which approximated the size of the original side chain but which is of different shape and flexibility, was also substituted at most of the same sites. Mutations that substantially destabilize the protein and are located in the carboxy-terminal domain generally slow the rate of folding. Destabilizing mutations in the amino-terminal domain, however, have little effect on the rate of folding. Mutations that have little effect on stability tend to have little effect on the rate, no matter where they are located. These results suggest that, at the rate-limiting step, elements of structure in the C-terminal domain are formed and have a structure similar to that of the fully folded protein. Consistent with this, two variants that somewhat increase the rate of folding (Phe104 --> Met and Val149 --> Met) are located within the carboxy-terminal domain and maintain or improve packing with very little perturbation of the wild-type structure. Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxy-terminal domain of T4 lysozyme is a rate-limiting step in folding.,Gassner NC, Baase WA, Lindstrom JD, Lu J, Dahlquist FW, Matthews BW Biochemistry. 1999 Nov 2;38(44):14451-60. PMID:10545167[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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