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| | <StructureSection load='5ex2' size='340' side='right'caption='[[5ex2]], [[Resolution|resolution]] 1.29Å' scene=''> | | <StructureSection load='5ex2' size='340' side='right'caption='[[5ex2]], [[Resolution|resolution]] 1.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ex2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hirbi Hirbi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EX2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EX2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ex2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirschia_baltica_ATCC_49814 Hirschia baltica ATCC 49814]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EX2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.294Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hbal_1421 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=582402 HIRBI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=5ex2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ex2 OCA], [https://pdbe.org/5ex2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ex2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ex2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ex2 ProSAT]</span></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=5ex2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ex2 OCA], [http://pdbe.org/5ex2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ex2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ex2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ex2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/C6XJ17_HIRBI C6XJ17_HIRBI] |
| | <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: Hirbi]] | + | [[Category: Hirschia baltica ATCC 49814]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidylprolyl isomerase]]
| + | [[Category: Jakob RP]] |
| - | [[Category: Jakob, R P]] | + | [[Category: Maier T]] |
| - | [[Category: Maier, T]] | + | |
| - | [[Category: Cyclophilin]]
| + | |
| - | [[Category: Folding helper]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Periplasmic]]
| + | |
| - | [[Category: Ppiase]]
| + | |
| - | [[Category: Rotamase]]
| + | |
| Structural highlights
Function
C6XJ17_HIRBI
Publication Abstract from PubMed
Cyclophilins are ubiquitous cis-trans-prolyl isomerases (PPIases) found in all kingdoms of life. Here, we identify a novel family of cyclophilins, termed AquaCyps, which specifically occurs in marine Alphaproteobacteria, but not in related terrestric species. In addition to a canonical PPIase domain, AquaCyps contain large extensions and insertions. The crystal structures of two representatives from Hirschia baltica, AquaCyp293 and AquaCyp300, reveal the formation of a compact domain, the NIC domain, by the N- and C-terminal extensions together with a central insertion. The NIC domain adopts a novel mixed alpha-helical, beta-sheet fold that is linked to the cyclophilin domain via a conserved disulfide bond. In its overall fold, AquaCyp293 resembles AquaCyp300, but the two proteins utilize distinct sets of active site residues, consistent with differences in their PPIase catalytic properties. While AquaCyp293 is a highly active general PPIase, AquaCyp300 is specific for hydrophobic substrate peptides and exhibits lower overall activity.
Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps.,Jakob RP, Schmidpeter PA, Koch JR, Schmid FX, Maier T PLoS One. 2016 Jun 8;11(6):e0157070. doi: 10.1371/journal.pone.0157070., eCollection 2016. PMID:27276069[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jakob RP, Schmidpeter PA, Koch JR, Schmid FX, Maier T. Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps. PLoS One. 2016 Jun 8;11(6):e0157070. doi: 10.1371/journal.pone.0157070., eCollection 2016. PMID:27276069 doi:http://dx.doi.org/10.1371/journal.pone.0157070
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