|
|
| Line 3: |
Line 3: |
| | <StructureSection load='6ait' size='340' side='right'caption='[[6ait]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='6ait' size='340' side='right'caption='[[6ait]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ait]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AIT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ait]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AIT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.598Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bepA, yfgC, b2494, JW2479 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6ait FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ait OCA], [http://pdbe.org/6ait PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ait RCSB], [http://www.ebi.ac.uk/pdbsum/6ait PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ait 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=6ait FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ait OCA], [https://pdbe.org/6ait PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ait RCSB], [https://www.ebi.ac.uk/pdbsum/6ait PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ait ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BEPA_ECOLI BEPA_ECOLI]] Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions.[HAMAP-Rule:MF_00997]<ref>PMID:22491786</ref> <ref>PMID:24003122</ref> | + | [https://www.uniprot.org/uniprot/BEPA_ECOLI BEPA_ECOLI] Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions.[HAMAP-Rule:MF_00997]<ref>PMID:22491786</ref> <ref>PMID:24003122</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kamikubo, H]] | + | [[Category: Kamikubo H]] |
| - | [[Category: Tanaka, Y]] | + | [[Category: Tanaka Y]] |
| - | [[Category: Tsukazaki, T]] | + | [[Category: Tsukazaki T]] |
| - | [[Category: Umar, M S.M]] | + | [[Category: Umar MSM]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| Structural highlights
Function
BEPA_ECOLI Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state. Promotes disulfide rearrangement of LptD during its biogenesis, and proteolytic degradation of LptD and BamA when their proper assembly is compromised. May facilitate membrane attachment of LoiP under unfavorable conditions.[HAMAP-Rule:MF_00997][1] [2]
Publication Abstract from PubMed
The beta-barrel assembly machinery (BAM) complex mediates the assembly of beta-barrel membrane proteins in the outer membrane. BepA, formerly known as YfgC, interacts with the BAM complex and functions as a protease/chaperone for the enhancement of the assembly and/or degradation of beta-barrel membrane proteins. To elucidate the molecular mechanism underlying the dual functions of BepA, its full-length three-dimensional structure is needed. Here, we report the crystal structure of full-length BepA at 2.6-A resolution. BepA possesses an N-terminal protease domain and a C-terminal tetratricopeptide repeat domain, which interact with each other. Domain cross-linking by structure-guided introduction of disulfide bonds did not affect the activities of BepA in vivo, suggesting that the function of this protein does not involve domain rearrangement. The full-length BepA structure is compatible with the previously proposed docking model of BAM complex and tetratricopeptide repeat domain of BepA.
Structural Basis for the Function of the beta-Barrel Assembly-Enhancing Protease BepA.,Shahrizal M, Daimon Y, Tanaka Y, Hayashi Y, Nakayama S, Iwaki S, Narita SI, Kamikubo H, Akiyama Y, Tsukazaki T J Mol Biol. 2018 Dec 3. pii: S0022-2836(18)31008-8. doi:, 10.1016/j.jmb.2018.11.024. PMID:30521812[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lutticke C, Hauske P, Lewandrowski U, Sickmann A, Kaiser M, Ehrmann M. E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds. Mol Biosyst. 2012 Jun;8(6):1775-82. doi: 10.1039/c2mb05506f. Epub 2012 Apr 11. PMID:22491786 doi:http://dx.doi.org/10.1039/c2mb05506f
- ↑ Narita S, Masui C, Suzuki T, Dohmae N, Akiyama Y. Protease homolog BepA (YfgC) promotes assembly and degradation of beta-barrel membrane proteins in Escherichia coli. Proc Natl Acad Sci U S A. 2013 Sep 17;110(38):E3612-21. doi:, 10.1073/pnas.1312012110. Epub 2013 Sep 3. PMID:24003122 doi:http://dx.doi.org/10.1073/pnas.1312012110
- ↑ Shahrizal M, Daimon Y, Tanaka Y, Hayashi Y, Nakayama S, Iwaki S, Narita SI, Kamikubo H, Akiyama Y, Tsukazaki T. Structural Basis for the Function of the beta-Barrel Assembly-Enhancing Protease BepA. J Mol Biol. 2018 Dec 3. pii: S0022-2836(18)31008-8. doi:, 10.1016/j.jmb.2018.11.024. PMID:30521812 doi:http://dx.doi.org/10.1016/j.jmb.2018.11.024
|
