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| | ==Clavulanic acid biosynthesis oligopeptide binding protein 2 complexed with bradykinin== | | ==Clavulanic acid biosynthesis oligopeptide binding protein 2 complexed with bradykinin== |
| - | <StructureSection load='2wok' size='340' side='right' caption='[[2wok]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='2wok' size='340' side='right'caption='[[2wok]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2wok]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1611 As 4.1611]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WOK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WOK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wok]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WOK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WOK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wol|2wol]], [[2wop|2wop]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=2wok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wok OCA], [http://pdbe.org/2wok PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wok RCSB], [http://www.ebi.ac.uk/pdbsum/2wok PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wok 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=2wok FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wok OCA], [https://pdbe.org/2wok PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wok RCSB], [https://www.ebi.ac.uk/pdbsum/2wok PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wok ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | == Disease == | |
| - | [[http://www.uniprot.org/uniprot/KNG1_HUMAN KNG1_HUMAN]] Congenital high-molecular-weight kininogen deficiency. The disease is caused by mutations affecting the gene represented in this entry. | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KNG1_HUMAN KNG1_HUMAN]] (1) Kininogens are inhibitors of thiol proteases; (2) HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects: (4A) influence in smooth muscle contraction, (4B) induction of hypotension, (4C) natriuresis and diuresis, (4D) decrease in blood glucose level, (4E) it is a mediator of inflammation and causes (4E1) increase in vascular permeability, (4E2) stimulation of nociceptors (4E3) release of other mediators of inflammation (e.g. prostaglandins), (4F) it has a cardioprotective effect (directly via bradykinin action, indirectly via endothelium-derived relaxing factor action); (5) LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting. | + | [https://www.uniprot.org/uniprot/Q8KRB4_STRCL Q8KRB4_STRCL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Oligopeptide-binding protein|Oligopeptide-binding protein]] | + | *[[ABC transporter 3D structures|ABC transporter 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: As 4 1611]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Andersson, I]] | + | [[Category: Large Structures]] |
| - | [[Category: Caines, M E.C]] | + | [[Category: Streptomyces clavuligerus]] |
| - | [[Category: Iqbal, A]] | + | [[Category: Andersson I]] |
| - | [[Category: Jensen, S E]] | + | [[Category: Caines MEC]] |
| - | [[Category: Kershaw, N J]] | + | [[Category: Iqbal A]] |
| - | [[Category: Mackenzie, A K]]
| + | [[Category: Jensen SE]] |
| - | [[Category: Schofield, C J]] | + | [[Category: Kershaw NJ]] |
| - | [[Category: Valegard, K]] | + | [[Category: Mackenzie AK]] |
| - | [[Category: Bradykinin]] | + | [[Category: Schofield CJ]] |
| - | [[Category: Clavulanic acid biosynthesis]] | + | [[Category: Valegard K]] |
| - | [[Category: Oligopeptide]] | + | |
| - | [[Category: Oligopeptide binding protein]]
| + | |
| - | [[Category: Peptide binding protein-peptide complex]]
| + | |
| - | [[Category: Solute-binding protein]]
| + | |
| Structural highlights
Function
Q8KRB4_STRCL
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
Clavulanic acid (CA) is a clinically important beta-lactamase inhibitor that is produced by fermentation of Streptomyces clavuligerus. The CA biosynthesis pathway starts from arginine and glyceraldehyde-3-phosphate and proceeds via (3S,5S)-clavaminic acid, which is converted to (3R,5R)-clavaldehyde, the immediate precursor of (3R,5R)-CA. Open reading frames 7 (orf7) and 15 (orf15) of the CA biosynthesis cluster encode oligopeptide-binding proteins (OppA1 and OppA2), which are essential for CA biosynthesis. OppA1/2 are proposed to be involved in the binding and/or transport of peptides across the S. clavuligerus cell membrane. Peptide binding assays reveal that recombinant OppA1 and OppA2 bind di-/tripeptides containing arginine and certain nonapeptides including bradykinin. Crystal structures of OppA2 in its apo form and in complex with arginine or bradykinin were solved to 1.45, 1.7, and 1.7 A resolution, respectively. The overall fold of OppA2 consists of two lobes with a deep cavity in the center, as observed for other oligopeptide-binding proteins. The large cavity creates a peptide/arginine binding cleft. The crystal structures of OppA2 in complex with arginine or bradykinin reveal that the C-terminal arginine of bradykinin binds similarly to arginine. The results are discussed in terms of the possible roles of OppA1/2 in CA biosynthesis.
Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid.,Mackenzie AK, Valegard K, Iqbal A, Caines ME, Kershaw NJ, Jensen SE, Schofield CJ, Andersson I J Mol Biol. 2010 Feb 19;396(2):332-44. Epub 2009 Nov 24. PMID:19941870[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mackenzie AK, Valegard K, Iqbal A, Caines ME, Kershaw NJ, Jensen SE, Schofield CJ, Andersson I. Crystal structures of an oligopeptide-binding protein from the biosynthetic pathway of the beta-lactamase inhibitor clavulanic acid. J Mol Biol. 2010 Feb 19;396(2):332-44. Epub 2009 Nov 24. PMID:19941870 doi:10.1016/j.jmb.2009.11.045
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