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| - | [[Image:3q6b.jpg|left|200px]] | |
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| - | <!--
| + | ==The high-resolution and new form crystal structure of BamA POTRA4-5 from E.coli== |
| - | The line below this paragraph, containing "STRUCTURE_3q6b", creates the "Structure Box" on the page.
| + | <StructureSection load='3q6b' size='340' side='right'caption='[[3q6b]], [[Resolution|resolution]] 1.50Å' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3q6b]] is a 1 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=3Q6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q6B FirstGlance]. <br> |
| - | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</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=3q6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q6b OCA], [https://pdbe.org/3q6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q6b RCSB], [https://www.ebi.ac.uk/pdbsum/3q6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q6b ProSAT]</span></td></tr> |
| - | {{STRUCTURE_3q6b| PDB=3q6b | SCENE= }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/BAMA_ECOLI BAMA_ECOLI] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.<ref>PMID:15951436</ref> <ref>PMID:16102012</ref> <ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21823654</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | In Escherichia coli, the BAM complex is employed to mediate correct folding of the outer membrane (OM) proteins into beta-barrels and their insertion into the OM. BamA, which is an essential component of the complex, consists of a C-terminal transmembrane region and five N-terminal polypeptide transport-associated (POTRA) domains. Although deletion studies have shown that each of the POTRA domains plays an important role in the process of BAM complex formation, only POTRA5 is essential for cell viability. Here, the crystal structure of POTRA4-5 has been determined to 1.50 A resolution with an R factor of 14.7% and an R(free) of 18.9%. |
| | | | |
| - | ===The high-resolution and new form crystal structure of BamA POTRA4-5 from E.coli===
| + | High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli.,Zhang H, Gao ZQ, Hou HF, Xu JH, Li LF, Su XD, Dong YH Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt, 7):734-8. Epub 2011 Jun 23. PMID:21795783<ref>PMID:21795783</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 3q6b" style="background-color:#fffaf0;"></div> |
| | | | |
| - | <!--
| + | ==See Also== |
| - | The line below this paragraph, {{ABSTRACT_PUBMED_21795783}}, adds the Publication Abstract to the page
| + | *[[Bam complex 3D structures|Bam complex 3D structures]] |
| - | (as it appears on PubMed at http://www.pubmed.gov), where 21795783 is the PubMed ID number.
| + | == References == |
| - | -->
| + | <references/> |
| - | {{ABSTRACT_PUBMED_21795783}}
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==About this Structure== | + | [[Category: Escherichia coli K-12]] |
| - | [[3q6b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q6B OCA]. | + | [[Category: Large Structures]] |
| - | | + | [[Category: Dong YH]] |
| - | ==Reference== | + | [[Category: Gao ZQ]] |
| - | <ref group="xtra">PMID:021795783</ref><references group="xtra"/> | + | [[Category: Zhang H]] |
| - | [[Category: Escherichia coli]] | + | |
| - | [[Category: Dong, Y H.]] | + | |
| - | [[Category: Gao, Z Q.]] | + | |
| - | [[Category: Zhang, H.]] | + | |
| - | [[Category: Insertion of outer membrane protein]] | + | |
| - | [[Category: Potra fold]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
BAMA_ECOLI Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
In Escherichia coli, the BAM complex is employed to mediate correct folding of the outer membrane (OM) proteins into beta-barrels and their insertion into the OM. BamA, which is an essential component of the complex, consists of a C-terminal transmembrane region and five N-terminal polypeptide transport-associated (POTRA) domains. Although deletion studies have shown that each of the POTRA domains plays an important role in the process of BAM complex formation, only POTRA5 is essential for cell viability. Here, the crystal structure of POTRA4-5 has been determined to 1.50 A resolution with an R factor of 14.7% and an R(free) of 18.9%.
High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli.,Zhang H, Gao ZQ, Hou HF, Xu JH, Li LF, Su XD, Dong YH Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt, 7):734-8. Epub 2011 Jun 23. PMID:21795783[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Doerrler WT, Raetz CR. Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant. J Biol Chem. 2005 Jul 29;280(30):27679-87. Epub 2005 Jun 10. PMID:15951436 doi:http://dx.doi.org/M504796200
- ↑ Werner J, Misra R. YaeT (Omp85) affects the assembly of lipid-dependent and lipid-independent outer membrane proteins of Escherichia coli. Mol Microbiol. 2005 Sep;57(5):1450-9. PMID:16102012 doi:http://dx.doi.org/MMI4775
- ↑ Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, Misra R, Silhavy TJ. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol Microbiol. 2006 Jul;61(1):151-64. PMID:16824102 doi:http://dx.doi.org/10.1111/j.1365-2958.2006.05211.x
- ↑ Hagan CL, Kim S, Kahne D. Reconstitution of outer membrane protein assembly from purified components. Science. 2010 May 14;328(5980):890-2. doi: 10.1126/science.1188919. Epub 2010 Apr, 8. PMID:20378773 doi:10.1126/science.1188919
- ↑ Hagan CL, Kahne D. The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of beta-barrel assembly. Biochemistry. 2011 Sep 6;50(35):7444-6. doi: 10.1021/bi2010784. Epub 2011 Aug 11. PMID:21823654 doi:10.1021/bi2010784
- ↑ Zhang H, Gao ZQ, Hou HF, Xu JH, Li LF, Su XD, Dong YH. High-resolution structure of a new crystal form of BamA POTRA4-5 from Escherichia coli. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt, 7):734-8. Epub 2011 Jun 23. PMID:21795783 doi:10.1107/S1744309111014254
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