Structure of PDB 5n8o Chain A

Receptor sequence

>5n8oA (length=1432) Species: 562 (Escherichia coli)

MMSIAQVRSAGSAGNYYTDKDNYYVLGSMGERWAGKGAEQLGLQGSVDKD
VFTRLLEGRLPDGADLSRMQDGSNKHRPGYDLTFSAPKSVSMMAMLGGDK
RLIDAHNQAVDFAVRQVEALASTRVMTDGQSETVLTGNLVMALFNHDTSR
DQEPQLHTHAVVANVTQHNGEWKTLSSDKVGKTGFIENVYANQIAFGRLY
REKLKEQVEALGYETEVVGKHGMWEMPGVPVEAFSVDPEIRMAEWMQTLK
ETGFDIRAYRDAADQRTEIRTQAPDVQQAVTQAIAGLSERKVQFTYTDVL
ARTVGILPPENGVIERARAGIDEAISREQLIPLDREKGLFTSGIHVLDEL
SVRALSRDIMKQNRVTVHPEKSVPRTAGYSDAVSVLAQDRPSLAIVSGQG
GAAGQRERVAELVMMAREQGREVQIIAADRRSQMNLKQDERLSGELITGR
RQLLEGMAFTPGSTVIVDQGEKLSLKETLTLLDGAARHNVQVLITDSGQR
TGTGSALMAMKDAGVNTYRWQGGEQRPATIISEPDRNVRYARLAGDFAAS
VKAGEESVAQVSGVREQAILTQAIRSELKTQGVLGHPEVTMTALSPVWLD
SRSRYLRDMYRPGMVMEQWNPETRSHDRYVIDRVTAQSHSLTLRDAQGET
QVVRISSLDSSWSLFRPEKMPVADGERLRVTGKIPGLRVSGGDRLQVASV
SEDAMTVVVPGRAEPASLPVSDSPFTALKLENGWVETPGHSVSDSATVFA
SVTQMAMNATLNGLARSGRDVRLYSSLDETRTAEKLARHPSFTVVSEQIK
ARAGETLLETAISLQKAGLHTPAQQAIHLALPVLESKNLAFSMVDLLTEA
KSFAAEGTGFTELGGEINAQIKRGDLLYVDVAKGYGTGLLVSRASYEAEK
SILRHILEGKEAVTPLMERVPGELMETLTSGQRAATRMILETSDRFTVVQ
GYAGVGKTTQFRAVMSAVNMLPASERPRVVGLGPTHRAVGEMRSAGVDAQ
TLASFLHDTQLQQRSGETPDFSNTLFLLDESSMVGNTEMARAYALIAAGG
GRAVASGDTDQLQAIAPGQSFRLQQTRSAADVVIMKEIVRQTPELREAVY
SLINRDVERALSGLESVKPSQVPRLEGAWAPEHSVTEFSHSQEAKLAEAQ
QKAMLKGEAFPDIPMTLYEAIVRDYTGRTPEAREQTLIVTHLNEDRRVLN
SMIHDAREKAGELGKEQVMVPVLNTANIRDGELRRLSTWEKNPDALALVD
NVYHRIAGISKDDGLITLQDAEGNTRLISPREAVAEGVTLYTPDKIRVGT
GDRMRFTKSDRERGYVANSVWTVTAVSGDSVTLSDGQQTRVIRPGQERAE
QHIDLAYAITAHGAQGASETFAIALEGTEGNRKLMAGFESAYVALSRMKQ
HVQVYTDNRQGWTDAINNAVQKGTAHDVLEPK

3D structure

• PDB: 5n8o Cryo-EM Structure of a Relaxase Reveals the Molecular Basis of DNA Unwinding during Bacterial Conjugation
• Chain: A
• Resolution: 3.9 Å

Enzymatic activity

• Enzyme Commision number: 3.6.4.12: DNA helicase.
  5.6.2.1: DNA topoisomerase.

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	dna	A	K179 Y190 I194 H221 Q333 D469 R470 T543 W638 T721 G722 K723 M795 S832 F833 P1025 T1026 H1027 A1044 S1045 H1048 A1105 I1106 L1233 R1352 H1403 R1423 K1424 M1426	K179 Y190 I194 H221 Q293 D429 R430 T503 W598 T681 G682 K683 M755 S791 F792 P984 T985 H986 A1003 S1004 H1007 A1064 I1065 L1192 R1311 H1362 R1382 K1383 M1385

Gene Ontology

Molecular Function

• GO:0003677 DNA binding
• GO:0003678 DNA helicase activity
• GO:0003917 DNA topoisomerase type I (single strand cut, ATP-independent) activity
• GO:0004386 helicase activity
• GO:0005524 ATP binding
• GO:0016787 hydrolase activity
• GO:0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
• GO:0016853 isomerase activity
• GO:0016887 ATP hydrolysis activity
• GO:0046872 metal ion binding

Biological Process

• GO:0032508 DNA duplex unwinding

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:5n8o, PDBe:5n8o, PDBj:5n8o
• PDBsum: 5n8o
• PubMed: 28457609
• UniProt: P14565|TRAI1_ECOLI Multifunctional conjugation protein TraI (Gene Name=traI)