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| | <StructureSection load='2pef' size='340' side='right'caption='[[2pef]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='2pef' size='340' side='right'caption='[[2pef]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2pef]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cals4 Cals4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2PEF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2pef]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caldanaerobacter_subterraneus_subsp._tengcongensis_MB4 Caldanaerobacter subterraneus subsp. tengcongensis MB4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PEF FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pee|2pee]]</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]] 1.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2pef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pef OCA], [http://pdbe.org/2pef PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pef RCSB], [http://www.ebi.ac.uk/pdbsum/2pef PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pef 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=2pef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pef OCA], [https://pdbe.org/2pef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pef RCSB], [https://www.ebi.ac.uk/pdbsum/2pef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pef ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8R9P5_CALS4 Q8R9P5_CALS4] |
| | == 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: Cals4]] | + | [[Category: Caldanaerobacter subterraneus subsp. tengcongensis MB4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Buckle, A M]] | + | [[Category: Buckle AM]] |
| - | [[Category: Whisstock, J C]] | + | [[Category: Whisstock JC]] |
| - | [[Category: Zhang, Q W]] | + | [[Category: Zhang QW]] |
| - | [[Category: Protease inhibitor]]
| + | |
| - | [[Category: Serpin]]
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| Structural highlights
Function
Q8R9P5_CALS4
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 PubMed
Serpins fold to a metastable native state and are susceptible to undergoing spontaneous conformational change to more stable conformers, such as the latent form. We investigated conformational change in tengpin, an unusual prokaryotic serpin from the extremophile Thermoanaerobacter tengcongensis. In addition to the serpin domain, tengpin contains a functionally uncharacterized 56-amino-acid amino-terminal region. Deletion of this domain creates a variant--tengpinDelta51--which folds past the native state and readily adopts the latent conformation. Analysis of crystal structures together with mutagenesis studies show that the N terminus of tengpin protects a hydrophobic patch in the serpin domain and functions to trap tengpin in its native metastable state. A 13-amino-acid peptide derived from the N terminus is able to mimick the role of the N terminus in stabilizing the native state of tengpinDelta51. Therefore, the function of the N terminus in tengpin resembles protein cofactors that prevent mammalian serpins from spontaneously adopting the latent conformation.
The N terminus of the serpin, tengpin, functions to trap the metastable native state.,Zhang Q, Buckle AM, Law RH, Pearce MC, Cabrita LD, Lloyd GJ, Irving JA, Smith AI, Ruzyla K, Rossjohn J, Bottomley SP, Whisstock JC EMBO Rep. 2007 Jul;8(7):658-63. Epub 2007 Jun 8. PMID:17557112[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang Q, Buckle AM, Law RH, Pearce MC, Cabrita LD, Lloyd GJ, Irving JA, Smith AI, Ruzyla K, Rossjohn J, Bottomley SP, Whisstock JC. The N terminus of the serpin, tengpin, functions to trap the metastable native state. EMBO Rep. 2007 Jul;8(7):658-63. Epub 2007 Jun 8. PMID:17557112
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