3PRW: Lipoprotein BamB

Crystal structure of the lipoprotein BamB. Determined by X-ray diffraction at 1.8 Å resolution. Released 19 Jan 2011.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Escherichia coli
Chains: 1
Atoms: 3,100
Mol. weight: 40.19 kDa
Released: 19 Jan 2011

Explore 3PRW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PRW contains 2 α-helices and 38 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 38 β-strands

Element	Residues	Length	Sheet
α-helix	32-37	6
β-strand	45-50	6	1
β-strand	66-68	3	2
β-strand	71-75	5	2
β-strand	80-85	6	2
β-strand	91-96	6	2
β-strand	99	1	3
β-strand	107	1	3
β-strand	111	1	4
β-strand	116-118	3	5
β-strand	121-125	5	5
β-strand	126	1	4
β-strand	130-135	6	5
β-strand	141-146	6	5
β-strand	156-157	2	6
β-strand	162-165	4	6
β-strand	170-174	5	6
β-strand	181-186	6	6
β-strand	201-203	3	7
β-strand	206-209	4	7
β-strand	215-220	6	7
β-strand	226-231	6	7
β-strand	252-254	3	8
β-strand	257-261	5	8
β-strand	267-271	5	8
β-strand	277-281	5	8
β-strand	288-292	5	9
β-strand	295-299	5	9
β-strand	305-309	5	9
β-strand	315-319	5	9
α-helix	327-330	4
β-strand	331-333	3	10
β-strand	336-340	5	10
β-strand	345-350	6	10
β-strand	356-361	6	10
β-strand	367	1	11
β-strand	372-374	3	1
β-strand	377-381	5	1
β-strand	382	1	11
β-strand	387-391	5	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lipoprotein yfgL	A	protein	377	Escherichia coli	P77774 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3PRW_1 Lipoprotein yfgL (chains A)
GPLGSSLFNSEEDVVKMSPLPTVENQFTPTTAWSTSVGSGIGNFYSNLHPALADNVVYAA
DRAGLVKALNADDGKEIWSVSLAEKDGWFSKEPALLSGGVTVSGGHVYIGSEKAQVYALN
TSDGTVAWQTKVAGEALSRPVVSDGLVLIHTSNGQLQALNEADGAVKWTVNLDMPSLSLR
GESAPTTAFGAAVVGGDNGRVSAVLMEQGQMIWQQRISQATGSTEIDRLSDVDTTPVVVN
GVVFALAYNGNLTALDLRSGQIMWKRELGSVNDFIVDGNRIYLVDQNDRVMALTIDGGVT
LWTQSDLLHRLLTSPVLYNGNLVVGDSEGYLHWINVEDGRFVAQQKVDSSGFQTEPVAAD
GKLLIQAKDGTVYSITR

Primary citation

Augmenting beta-augmentation: structural basis of how BamB binds BamA and may support folding of outer membrane proteins. Heuck, A., Schleiffer, A., Clausen, T. J Mol Biol (2011) 406:659-666. DOI 10.1016/j.jmb.2011.01.002 · PubMed

Other PDB entries of the same protein (UniProt P77774 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3Q7M 1.65 Å, The crystal structure of BamB from the BAM complex in spacegroup I222
3Q7N 1.77 Å, The crystal structure of BamB from the BAM complex in spacegroup P212121
3Q7O 2.09 Å, The crystal structure of BamB from the BAM complex in spacegroup P213
2YMS 2.1 Å, Structure and assembly of a b-propeller with nine blades and a new conserved repetitive…
4XGA 2.15 Å, Crystal structure of BamB and BamA P3-5 complex from E.coli
2YH3 2.6 Å, The structure of BamB from E. coli
3P1L 2.6 Å, Crystal structure of Escherichia coli BamB, a lipoprotein component of the beta-barrel…
9CNW 2.6 Å, CryoEM structure of the APO-BAM complex in DDM detergent
9HG6 2.73 Å, BAM-SurA complex in the swing-in state
9HG5 2.82 Å, BAM-SurA complex in the swing-in state with full length BamC resolved
9HG7 2.83 Å, BAM-SurA complex in the swing-out state
9HG9 2.88 Å, BAM-SurA-darobactin complex in the swing-in state

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