Modomics - A Database of RNA Modifications

ID Card:

Full name: DNA dC->dU-editing enzyme APOBEC-3G
GI: 44887683
UniProt: Q9HC16
Structures: | 2JYW | 2KBO | 2KEM | 3E1U | 3IQS | 3IR2 | 3V4J | 3V4K | 4ROV | 5ZVA | 5ZVB | 6BUX | 6BWY | 6K3J | 6K3K |
Alpha Fold Predicted Structure: AF-Q9HC16-F1
Enzyme type: deaminase


PDB Structures:


2JYW

Structure Description:

Title:
Classification:
Technique:

Abstract of the PDB Structure's related Publication:

The human APOBEC3G (apolipoprotein B messenger-RNA-editing enzyme, catalytic polypeptide-like 3G) protein is a single-strand DNA deaminase that inhibits the replication of human immunodeficiency virus-1 (HIV-1), other retroviruses and retrotransposons. APOBEC3G anti-viral activity is circumvented by most retroelements, such as through degradation by HIV-1 Vif. APOBEC3G is a member of a family of polynucleotide cytosine deaminases, several of which also target distinct physiological substrates. For instance, APOBEC1 edits APOB mRNA and AID deaminates antibody gene DNA. Although structures of other family members exist, none of these proteins has elicited polynucleotide cytosine deaminase or anti-viral activity. Here we report a solution structure of the human APOBEC3G catalytic domain. Five alpha-helices, including two that form the zinc-coordinating active site, are arranged over a hydrophobic platform consisting of five beta-strands. NMR DNA titration experiments, computational modelling, phylogenetic conservation and Escherichia coli-based activity assays combine to suggest a DNA-binding model in which a brim of positively charged residues positions the target cytosine for catalysis. The structure of the APOBEC3G catalytic domain will help us to understand functions of other family members and interactions that occur with pathogenic proteins such as HIV-1 Vif.

Download RCSB-PDB Structures:

Pdb Files   2JYW.pdb   2KBO.pdb   2KEM.pdb   3E1U.pdb   3IQS.pdb   3IR2.pdb   3V4J.pdb   3V4K.pdb   4ROV.pdb   5ZVA.pdb   5ZVB.pdb   6BUX.pdb   6BWY.pdb   6K3J.pdb   6K3K.pdb  
Pdbx/mmCIF Files   2JYW.cif   2KBO.cif   2KEM.cif   3E1U.cif   3IQS.cif   3IR2.cif   3V4J.cif   3V4K.cif   4ROV.cif   5ZVA.cif   5ZVB.cif   6BUX.cif   6BWY.cif   6K3J.cif   6K3K.cif  


Protein sequence:

MKPHFRNTVERMYRDTFSYNFYNRPILSRRNTVWLCYEVKTKGPSRPPLDAKIFRGQVYSELKYHPEMRFFHWFSKWRKLHRDQEYEVTWYISWSPCTKCTRDMATFLAEDPKVTLTIFVARLYYFWDPDYQEALRSLCQKRDGPRATMKIMNYDEFQHCWSKFVYSQRELFEPWNNLPKYYILLHIMLGEILRHSMDPPTFTFNFNNEPWVRGRHETYLCYEVERMHNDTWVLLNQRRGFLCNQAPHKHGFLEGRHAELCFLDVIPFWKLDLDQDYRVTCFTSWSPCFSCAQEMAKFISKNKHVSLCIFTARIYDDQGRCQEGLRTLAEAGAKISIMTYSEFKHCWDTFVDHQGCPFQPWDGLDEHSQDLSGRLRAILQNQEN

Comments:





Alpha Fold Predicted Structure:






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Protein sequence:

M K P H F R N T V E R M Y R D T F S Y N F Y N R P I L S R R N T V W L C Y E V K T K G P S R P P L D A K I F R G Q V Y S E L K Y H P E M R F F H W F S K W R K L H R D Q E Y E V T W Y I S W S P C T K C T R D M A T F L A E D P K V T L T I F V A R L Y Y F W D P D Y Q E A L R S L C Q K R D G P R A T M K I M N Y D E F Q H C W S K F V Y S Q R E L F E P W N N L P K Y Y I L L H I M L G E I L R H S M D P P T F T F N F N N E P W V R G R H E T Y L C Y E V E R M H N D T W V L L N Q R R G F L C N Q A P H K H G F L E G R H A E L C F L D V I P F W K L D L D Q D Y R V T C F T S W S P C F S C A Q E M A K F I S K N K H V S L C I F T A R I Y D D Q G R C Q E G L R T L A E A G A K I S I M T Y S E F K H C W D T F V D H Q G C P F Q P W D G L D E H S Q D L S G R L R A I L Q N Q E N

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-Q9HC16-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-Q9HC16-F1.cif  
DSSP Secondary Structures   Q9HC16.dssp  





Publications:

Title Authors Journal Details PubMed Id DOI