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| | <StructureSection load='3urc' size='340' side='right'caption='[[3urc]], [[Resolution|resolution]] 1.10Å' scene=''> | | <StructureSection load='3urc' size='340' side='right'caption='[[3urc]], [[Resolution|resolution]] 1.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3urc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29487 Atcc 29487]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3URC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3URC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3urc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3URC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3URC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ssx|1ssx]], [[2alp|2alp]], [[4sgb|4sgb]], [[2oua|2oua]], [[2pfe|2pfe]], [[3urd|3urd]], [[3ure|3ure]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alpha-LP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69 ATCC 29487])</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=3urc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3urc OCA], [https://pdbe.org/3urc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3urc RCSB], [https://www.ebi.ac.uk/pdbsum/3urc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3urc ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] </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=3urc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3urc OCA], [http://pdbe.org/3urc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3urc RCSB], [http://www.ebi.ac.uk/pdbsum/3urc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3urc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Alpha-lytic endopeptidase]] | |
| - | [[Category: Atcc 29487]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Agard, D A]] | + | [[Category: Lysobacter enzymogenes]] |
| - | [[Category: Kelch, B A]] | + | [[Category: Agard DA]] |
| - | [[Category: Hydrolase]] | + | [[Category: Kelch BA]] |
| - | [[Category: Serine protease]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Ultrahigh-resolution (< 1.0 A) structures have revealed unprecedented and unexpected details of molecular geometry, such as the deformation of aromatic rings from planarity. However, the functional utility of such energetically costly strain is unknown. The 0.83 A structure of alpha-lytic protease (alphaLP) indicated that residues surrounding a conserved Phe side-chain dictate a rotamer which results in a approximately 6 degrees distortion along the side-chain, estimated to cost 4 kcal/mol. By contrast, in the closely related protease Streptomyces griseus Protease B (SGPB), the equivalent Phe adopts a different rotamer and is undistorted. Here, we report that the alphaLP Phe side-chain distortion is both functional and conserved in proteases with large pro regions. Sequence analysis of the alphaLP serine protease family reveals a bifurcation separating those sequences expected to induce distortion and those that would not, which correlates with the extent of kinetic stability. Structural and folding kinetics analyses of family members suggest that distortion of this side-chain plays a role in increasing kinetic stability within the alphaLP family members that use a large Pro region. Additionally, structural and kinetic folding studies of mutants demonstrate that strain alters the folding free energy landscape by destabilizing the transition state (TS) relative to the native state (N). Although side-chain distortion comes at a cost of foldability, it suppresses the rate of unfolding, thereby enhancing kinetic stability and increasing protein longevity under harsh extracellular conditions. This ability of a structural distortion to enhance function is unlikely to be unique to alphaLP family members and may be relevant in other proteins exhibiting side-chain distortions.
Functional modulation of a protein folding landscape via side-chain distortion.,Kelch BA, Salimi NL, Agard DA Proc Natl Acad Sci U S A. 2012 Jun 12;109(24):9414-9. Epub 2012 May 25. PMID:22635267[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kelch BA, Salimi NL, Agard DA. Functional modulation of a protein folding landscape via side-chain distortion. Proc Natl Acad Sci U S A. 2012 Jun 12;109(24):9414-9. Epub 2012 May 25. PMID:22635267 doi:10.1073/pnas.1119274109
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