Structure of PDB 1xpu Chain C

Receptor sequence

>1xpuC (length=408) Species: 562 (Escherichia coli)

MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIF
GDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGK
IRPPKEGERYFALLKVNEVNFDKPENNKILFENLTPLHANSRLRMGSTED
LTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMV
LLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEH
KKDVIILLDSITRLARAYNTVVPAVLTGGVDANALHRPKRFFGAARNVEE
GGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAID
YNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTN
DDFFEMMK

3D structure

• PDB: 1xpu Structural mechanism of inhibition of the rho transcription termination factor by the antibiotic bicyclomycin
• Chain: C
• Resolution: 3.05 Å

Enzymatic activity

• Enzyme Commision number: 3.6.4.-

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	rna	C	F64 R66 G75 D78 Y80 E108 R109 Y110	F64 R66 G75 D78 Y80 E108 R109 Y110
BS02	MG	C	K184 T185 D265	K178 T179 D259
BS03	AGS	C	K181 G183 K184 T185 M186 F355	K175 G177 K178 T179 M180 F346
BS04	FPD	C	P180 K181 D210 E211 R212 D265 S266 R269 L320 T323	P174 K175 D204 E205 R206 D259 S260 R263 L311 T314
BS05	FPD	C	G337 E342	G328 E333

Gene Ontology

Molecular Function

• GO:0003676 nucleic acid binding
• GO:0003723 RNA binding
• GO:0004386 helicase activity
• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0008186 ATP-dependent activity, acting on RNA
• GO:0016787 hydrolase activity
• GO:0016887 ATP hydrolysis activity
• GO:0042802 identical protein binding

Biological Process

• GO:0006353 DNA-templated transcription termination

Cellular Component

• GO:0005829 cytosol
• GO:0016020 membrane

External links

• PDB: RCSB:1xpu, PDBe:1xpu, PDBj:1xpu
• PDBsum: 1xpu
• PubMed: 15642265
• UniProt: P0AG30|RHO_ECOLI Transcription termination factor Rho (Gene Name=rho)