|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5keh' size='340' side='right'caption='[[5keh]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='5keh' size='340' side='right'caption='[[5keh]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5keh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29906 Atcc 29906]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KEH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KEH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5keh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Proteus_mirabilis Proteus mirabilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KEH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4w8q|4w8q]], [[5kdk|5kdk]], [[5kf3|5kf3]]</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]] 1.551Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hpmA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=584 ATCC 29906])</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=5keh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5keh OCA], [https://pdbe.org/5keh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5keh RCSB], [https://www.ebi.ac.uk/pdbsum/5keh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5keh 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=5keh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5keh OCA], [http://pdbe.org/5keh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5keh RCSB], [http://www.ebi.ac.uk/pdbsum/5keh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5keh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HLYA_PROMI HLYA_PROMI] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 24: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 29906]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bhattacharyya, B]] | + | [[Category: Proteus mirabilis]] |
| - | [[Category: Novak, W R.P]] | + | [[Category: Bhattacharyya B]] |
| - | [[Category: Weaver, T M]] | + | [[Category: Novak WRP]] |
| - | [[Category: Beta helix]] | + | [[Category: Weaver TM]] |
| - | [[Category: Beta solenoid]]
| + | |
| - | [[Category: Hemolysin]]
| + | |
| - | [[Category: Toxin]]
| + | |
| - | [[Category: Two partner secretion]]
| + | |
| Structural highlights
Function
HLYA_PROMI
Publication Abstract from PubMed
Wild-type and variant forms of HpmA265 (truncated hemolysin A) from Proteus mirabilis reveal a right-handed, parallel beta-helix capped and flanked by segments of antiparallel beta-strands. The low-salt crystal structures form a dimeric structure via the implementation of on-edge main-chain hydrogen bonds donated by residues 243-263 of adjacent monomers. Surprisingly, in the high-salt structures of two variants, Y134A and Q125A-Y134A, a new dimeric interface is formed via main-chain hydrogen bonds donated by residues 203-215 of adjacent monomers, and a previously unobserved tetramer is formed. In addition, an eight-stranded antiparallel beta-sheet is formed from the flap regions of crystallographically related monomers in the high-salt structures. This new interface is possible owing to additional proteolysis of these variants after Tyr240. The interface formed in the high-salt crystal forms of hemolysin A variants may mimic the on-edge beta-strand positioning used in template-assisted hemolytic activity.
Proteolysis of truncated hemolysin A yields a stable dimerization interface.,Novak WR, Bhattacharyya B, Grilley DP, Weaver TM Acta Crystallogr F Struct Biol Commun. 2017 Mar 1;73(Pt 3):138-145. doi:, 10.1107/S2053230X17002102. Epub 2017 Feb 21. PMID:28291749[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Novak WR, Bhattacharyya B, Grilley DP, Weaver TM. Proteolysis of truncated hemolysin A yields a stable dimerization interface. Acta Crystallogr F Struct Biol Commun. 2017 Mar 1;73(Pt 3):138-145. doi:, 10.1107/S2053230X17002102. Epub 2017 Feb 21. PMID:28291749 doi:http://dx.doi.org/10.1107/S2053230X17002102
|
