3p1l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:37, 21 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3p1l' size='340' side='right'caption='[[3p1l]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3p1l' size='340' side='right'caption='[[3p1l]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3p1l]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P1L FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3p1l]] 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=3P1L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P1L FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.6&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2512, JW2496, yfgL ([https://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=NA:SODIUM+ION'>NA</scene></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=3p1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p1l OCA], [https://pdbe.org/3p1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p1l RCSB], [https://www.ebi.ac.uk/pdbsum/3p1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p1l 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=3p1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p1l OCA], [https://pdbe.org/3p1l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p1l RCSB], [https://www.ebi.ac.uk/pdbsum/3p1l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p1l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/BAMB_ECOLI BAMB_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, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins.<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:21586578</ref> <ref>PMID:21277859</ref>
+
[https://www.uniprot.org/uniprot/BAMB_ECOLI BAMB_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, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins.<ref>PMID:20378773</ref> <ref>PMID:21823654</ref> <ref>PMID:21586578</ref> <ref>PMID:21277859</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
In Gram-negative bacteria, the BAM (beta-barrel assembly machinery) complex catalyzes the essential process of assembling outer membrane proteins. The BAM complex in Escherichia coli consists of five proteins: one beta-barrel membrane protein, BamA, and four lipoproteins, BamB, BamC, BamD, and BamE. Despite their role in outer membrane protein biogenesis, there is currently a lack of functional and structural information on the lipoprotein components of the BAM complex. Here, we report the first crystal structure of BamB, the largest and most functionally characterized lipoprotein component of the BAM complex. The crystal structure shows that BamB has an eight-bladed beta-propeller structure, with four beta-strands making up each blade. Mapping onto the structure the residues previously shown to be important for BamA interaction reveals that these residues, despite being far apart in the amino acid sequence, are localized to form a continuous solvent-exposed surface on one side of the beta-propeller. Found on the same side of the beta-propeller is a cluster of residues conserved among BamB homologs. Interestingly, our structural comparison study suggests that other proteins with a BamB-like fold often participate in protein or ligand binding, and that the binding interface on these proteins is located on the surface that is topologically equivalent to where the conserved residues and the residues that are important for BamA interaction are found on BamB. Our structural and bioinformatic analyses, together with previous biochemical data, provide clues to where the BamA and possibly a substrate interaction interface may be located on BamB.
+
-
 
+
-
Crystal Structure of Escherichia coli BamB, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex.,Kim KH, Paetzel M J Mol Biol. 2010 Dec 17. PMID:21168416<ref>PMID:21168416</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3p1l" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
Line 26: Line 17:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Ecoli]]
+
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Kim, K H]]
+
[[Category: Kim KH]]
-
[[Category: Paetzel, M]]
+
[[Category: Paetzel M]]
-
[[Category: Beta propeller]]
+
-
[[Category: Lipoprotein involved in beta-barrel assembly in e. coli]]
+
-
[[Category: Protein binding]]
+

Current revision

Crystal structure of Escherichia coli BamB, a lipoprotein component of the beta-barrel assembly machinery complex, native crystals.

PDB ID 3p1l

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3p1l"
Personal tools