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| | <StructureSection load='5ez1' size='340' side='right'caption='[[5ez1]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='5ez1' size='340' side='right'caption='[[5ez1]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ez1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EZ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ez1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EZ1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ICB:1H-INDOLE-2-CARBOXYLIC+ACID'>ICB</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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0175 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ICB:1H-INDOLE-2-CARBOXYLIC+ACID'>ICB</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=5ez1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ez1 OCA], [https://pdbe.org/5ez1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ez1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ez1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ez1 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=5ez1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ez1 OCA], [http://pdbe.org/5ez1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ez1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ez1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ez1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Y175_HELPY Y175_HELPY] |
| - | Helicobacter pylori cell binding factor 2 (HpCBF2) is an antigenic virulence factor belonging to the SurA-like peptidyl-prolyl cis-trans isomerase family with implications for pathogenicity in the human gastrointestinal tract. HpCBF2 possesses PPIase activity and could act as a periplasmic chaperone to regulate outer membrane protein assembly. Here, we measured the isomerization and chaperone activity of HpCBF2, and determined the crystal structure of HpCBF2 in complex with an inhibitor, indole-2-carboxylic acid (I2CA), at 2.4A resolution. HpCBF2-I2CA forms a homodimer encasing a large central hydrophobic cavity with a basket-like structure, and each monomer contains a PPIase and a chaperone domain. In the HpCBF2-I2CA dimer, the two PPIase domains separate by a distance of 22.8A, while the two chaperone domains arrange in a domain-swap manner. The PPIase domains bound with I2CA ligand face towards the chaperone domains and are shielded by surrounding hydrophobic residues. With the aid of SAXS experiments, we also revealed domain motion between the apo- and I2CA-bound states of HpCBF2. The domain motion in HpCBF2 might be necessary for the isomerization activity of PPIase and the accommodation of the unfolded and partially folded peptides to refold by chaperone domain.
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| - | Helicobacter pylori cell binding factor 2: Insights into domain motion.,Naveen V, Chu CH, Chen BW, Tsai YC, Hsiao CD, Sun YJ J Struct Biol. 2016 Apr;194(1):90-101. doi: 10.1016/j.jsb.2016.02.002. Epub 2016 , Feb 2. PMID:26850168<ref>PMID:26850168</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 5ez1" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Peptidylprolyl isomerase]]
| + | [[Category: Chu CH]] |
| - | [[Category: Chu, C H]] | + | [[Category: Sun YJ]] |
| - | [[Category: Sun, Y J]] | + | [[Category: Tsai YC]] |
| - | [[Category: Tsai, Y C]] | + | |
| - | [[Category: Cell binding factor 2]]
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| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Peptidyl prolyl cis-trans isomerase]]
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