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| | ==Crystal structure of the E. coli BamCD complex== | | ==Crystal structure of the E. coli BamCD complex== |
| - | <StructureSection load='3tgo' size='340' side='right' caption='[[3tgo]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='3tgo' size='340' side='right'caption='[[3tgo]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3tgo]] is a 4 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=3TGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TGO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3tgo]] is a 4 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=3TGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TGO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yh6|2yh6]], [[2laf|2laf]], [[2yhc|2yhc]], [[3qky|3qky]], [[3sns|3sns]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2595, JW2577, yfiO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), b2477, dapX, JW2462, nlpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3tgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tgo OCA], [https://pdbe.org/3tgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tgo RCSB], [https://www.ebi.ac.uk/pdbsum/3tgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tgo 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=3tgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tgo OCA], [http://pdbe.org/3tgo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tgo RCSB], [http://www.ebi.ac.uk/pdbsum/3tgo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tgo ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BAMD_ECOLI BAMD_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 BamA, the core component of the assembly machinery. Probably involved in transient protein interactions.[HAMAP-Rule:MF_00922]<ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21586578</ref> <ref>PMID:21823654</ref> <ref>PMID:22281737</ref> [[http://www.uniprot.org/uniprot/BAMC_ECOLI BAMC_ECOLI]] Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD.[HAMAP-Rule:MF_00924]<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:22178970</ref> | + | [https://www.uniprot.org/uniprot/BAMD_ECOLI BAMD_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 BamA, the core component of the assembly machinery. Probably involved in transient protein interactions.[HAMAP-Rule:MF_00922]<ref>PMID:16824102</ref> <ref>PMID:20378773</ref> <ref>PMID:21586578</ref> <ref>PMID:21823654</ref> <ref>PMID:22281737</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | The beta-barrel assembly machinery (BAM) complex of Escherichia coli is a multiprotein machine that catalyzes the essential process of assembling outer membrane proteins. The BAM complex consists of five proteins: one membrane protein, BamA, and four lipoproteins, BamB, BamC, BamD, and BamE. Here, we report the first crystal structure of a Bam lipoprotein complex: the essential lipoprotein BamD in complex with the N-terminal half of BamC (BamC(UN) (Asp(28)-Ala(217)), a 73-residue-long unstructured region followed by the N-terminal domain). The BamCD complex is stabilized predominantly by various hydrogen bonds and salt bridges formed between BamD and the N-terminal unstructured region of BamC. Sequence and molecular surface analyses revealed that many of the conserved residues in both proteins are found at the BamC-BamD interface. A series of truncation mutagenesis and analytical gel filtration chromatography experiments confirmed that the unstructured region of BamC is essential for stabilizing the BamCD complex structure. The unstructured N terminus of BamC interacts with the proposed substrate-binding pocket of BamD, suggesting that this region of BamC may play a regulatory role in outer membrane protein biogenesis.
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| - | Crystal Structure of beta-Barrel Assembly Machinery BamCD Protein Complex.,Kim KH, Aulakh S, Paetzel M J Biol Chem. 2011 Nov 11;286(45):39116-21. Epub 2011 Sep 20. PMID:21937441<ref>PMID:21937441</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 3tgo" style="background-color:#fffaf0;"></div>
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Bam complex|Bam complex]] | + | *[[Bam complex 3D structures|Bam complex 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Aulakh, S]]
| + | [[Category: Large Structures]] |
| - | [[Category: Kim, K H]]
| + | [[Category: Aulakh S]] |
| - | [[Category: Paetzel, M]]
| + | [[Category: Kim KH]] |
| - | [[Category: Helix-grip fold]]
| + | [[Category: Paetzel M]] |
| - | [[Category: Lipoprotein complex]] | + | |
| - | [[Category: Membrane protein]] | + | |
| - | [[Category: Outer membrane]] | + | |
| - | [[Category: Outer membrane protein assembly]] | + | |
| - | [[Category: Tpr repeat]]
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