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| | <StructureSection load='4wwv' size='340' side='right'caption='[[4wwv]], [[Resolution|resolution]] 3.01Å' scene=''> | | <StructureSection load='4wwv' size='340' side='right'caption='[[4wwv]], [[Resolution|resolution]] 3.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wwv]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Desa1 Desa1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WWV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wwv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Desulfurococcus_amylolyticus_1221n Desulfurococcus amylolyticus 1221n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WWV FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xfo|1xfo]], [[1y0f|1y0f]]</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]] 3.006Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DKAM_0589 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=490899 DESA1])</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=4wwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wwv OCA], [https://pdbe.org/4wwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wwv RCSB], [https://www.ebi.ac.uk/pdbsum/4wwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wwv 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=4wwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wwv OCA], [http://pdbe.org/4wwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wwv RCSB], [http://www.ebi.ac.uk/pdbsum/4wwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wwv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B8D484_DESA1 B8D484_DESA1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Desa1]] | + | [[Category: Desulfurococcus amylolyticus 1221n]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Boyko, K M]] | + | [[Category: Boyko KM]] |
| - | [[Category: Gorbacheva, M A]] | + | [[Category: Gorbacheva MA]] |
| - | [[Category: Korzhenevskiy, D A]] | + | [[Category: Korzhenevskiy DA]] |
| - | [[Category: Petrova, T]] | + | [[Category: Petrova T]] |
| - | [[Category: Popov, V O]] | + | [[Category: Popov VO]] |
| - | [[Category: Rakitina, T V]] | + | [[Category: Rakitina TV]] |
| - | [[Category: Aminopeptidase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
B8D484_DESA1
Publication Abstract from PubMed
The crystal structure of the aminopeptidase APDkam589 from the thermophilic crenarchaeon Desulfurococcus kamchatkensis was determined at a resolution of 3.0 A. In the crystal, the monomer of APDkam589 and its symmetry-related monomers are densely packed to form a 12-subunit complex. Single-particle electron-microscopy analysis confirms that APDkam589 is present as a compact dodecamer in solution. The APDkam589 molecule is built similarly to the molecules of the PhTET peptidases, which have the highest sequence identity to APDkam589 among known structures and were isolated from the more thermostable archaeon Pyrococcus horikoshii. A comparison of the interactions of the subunits in APDkam589 with those in PhTET1, PhTET2 and PhTET3 reveals that APDkam589 has a much lower total number of salt bridges, which correlates with the lower thermostability of APDkam589. The monomer of APDkam589 has six Trp residues, five of which are on the external surface of the dodecamer. A superposition of the structure of APDkam589 with those having a high sequence similarity to APDkam589 reveals that, although the positions of Trp45, Trp252 and Trp358 are not conserved in the sequences, the spatial locations of the Trp residues in these models are similar.
Structure of the dodecamer of the aminopeptidase APDkam598 from the archaeon Desulfurococcus kamchatkensis.,Petrova TE, Slutskaya ES, Boyko KM, Sokolova OS, Rakitina TV, Korzhenevskiy DA, Gorbacheva MA, Bezsudnova EY, Popov VO Acta Crystallogr F Struct Biol Commun. 2015 Mar;71(Pt 3):277-85. doi:, 10.1107/S2053230X15000783. Epub 2015 Feb 19. PMID:25760701[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Petrova TE, Slutskaya ES, Boyko KM, Sokolova OS, Rakitina TV, Korzhenevskiy DA, Gorbacheva MA, Bezsudnova EY, Popov VO. Structure of the dodecamer of the aminopeptidase APDkam598 from the archaeon Desulfurococcus kamchatkensis. Acta Crystallogr F Struct Biol Commun. 2015 Mar;71(Pt 3):277-85. doi:, 10.1107/S2053230X15000783. Epub 2015 Feb 19. PMID:25760701 doi:http://dx.doi.org/10.1107/S2053230X15000783
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