Immunotation of Rv0058
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Revision as of 10:36, 5 February 2010
Immunotation of Rv0058
| |
Name | |
replicative DNA helicase | |
Identifiers | |
Swiss Prot | |
Genbank | |
PDB | |
Chemical data | |
Formula | ? |
Mol. wt. | 96915.7 Da |
Pharmacokinetic data | |
Bioavailability | ? |
Solubility | ? |
Isoelectric-Point | 8.81 |
Contents |
General
Hexameric DnaB helicase unwinds the DNA double helix during replication of genetic material in bacteria. DnaB is an essential bacterial protein; therefore, it is an important potential target for antibacterial drug discovery.A crystal structure of the N-terminal region of DnaB from the pathogen Mycobacterium tuberculosis (MtDnaBn), determined at 2.0 A resolution have been reported. This structure provides atomic resolution details of formation of the hexameric ring of DnaB by two distinct interfaces. An extensive hydrophobic interface stabilizes a dimer of MtDnaBn by forming a four-helix bundle. The other, less extensive, interface is formed between the dimers, connecting three of them into a hexameric ring. On the basis of crystal packing interactions between MtDnaBn rings,a model of a helicase-primase complex that explains previously observed effects of DnaB mutations on DNA priming have been suggested. A characterization of the physical interactions between M. tuberculosis DnaA and DnaB using both in vivo methods, such as bacterial two�hybrid assays, and in vitro techniques, such as surface plasmon resonance (SPR) and Pull�down/Western blotting. The full�length N�terminus (1�206 residues) of DnaB was found to interact with DnaA, while the shorter N�terminal domain of DnaB (1� 125 residues), which lacked the linker region, did not.
Protein Sequence
>Rv0058, TB.seq 60394:63015 MW:96919 MAVVDDLAPGMDSSPPSEDYGRQPPQDLAAEQSVLGGMLLSKDAIADVLERLRPGDFYRPAHQNVYDAILDLYGRGEPAD AVTVAAELDRRGLLRRIGGAPYLHTLISTVPTAANAGYYASIVAEKALLRRLVEAGTRVVQYGYAGAEGADVAEVVDRAQ AEIYDVADRRLSEDFVALEDLLQPTMDEIDAIASSGGLARGVATGFTELDEVTNGLHPGQMVIVAARPGVGKSTLGLDFM RSCSIRHRMASVIFSLEMSKSEIVMRLLSAEAKIKLSDMRSGRMSDDDWTRLARRMSEISEAPLFIDDSPNLTMMEIRAK ARRLRQKANLKLIVVDYLQLMTSGKKYESRQVEVSEFSRHLKLLAKELEVPVVAISQLNRGPEQRTDKKPMLADLRESGC LTASTRILRADTGAEVAFGELMRSGERPMVWSLDERLRMVARPMINVFPSGRKEVFRLRLASGREVEATGSHPFMKFEGW TPLAQLKVGDRIAAPRRVPEPIDTQRMPESELISLARMIGDGSCLKNQPIRYEPVDEANLAAVTVSAAHSDRAAIRDDYL AARVPSLRPARQRLPRGRCTPIAAWLAGLGLFTKRSHEKCVPEAVFRAPNDQVALFLRHLWSAGGSVRWDPTNGQGRVYY GSTSRRLIDDVAQLLLRVGIFSWITHAPKLGGHDSWRLHIHGAKDQVRFLRHVGVHGAEAVAAQEMLRQLKGPVRNPNLD SAPKKVWAQVRNRLSAKQMMDIQLHEPTMWKHSPSRSRPHRAEARIEDRAIHELARGDAYWDTVVEITSIGDQHVFDGTV SGTHNFVANGISLHNSLEQDADVVILLHRPDAFDRDDPRGGEADFILAKHRNGPTKTVTVAHQLHLSRFANMAR
Human Homologue Blast Result
subject ids | % identity | % positives | alignment length | evalue |
Alergen Protein
Link to Algpred
Non Allergen Predicted by AlgPred Server
Bacterial Toxin Prediction
Link to btxpred
No Hit Fountd by btxpred server.
Subcellular Location
Link to TBpred
Cyoplasmic
Antigens
No Hit Found in AntigenDB
No. Hit Found in IEDB
B cell Epitopes
BCEpred Analysis
Link to Bcepred
Result Predicited by []
ABCpred Analysis
Link to ABCpred
Result Predicited by []
IEDB Analysis
Link to IEDB
Result Predicited by []
MHC Class-I Binder
nHLAPred Analysis
Link to nHLApred
Result Predicited by []
IEDB Analysis
Link to IEDB
Result Predicted by []
MHC Class-II Binder
Propred Analysis
Link to Propred
Result Predicted by []
NetMHC-II Analysis
Link to NetMHC-II
Result Predicted by []
External Links
- Database of Mycobacterium tuberculosis genome sequences and related information.