Structural annotation of Rv2753c (dihydrodipicolinate synthase)
From DrugPedia: A Wikipedia for Drug discovery
| Structural annotation of Rv2753c (dihydrodipicolinate synthase)
| |
| Name | |
| Dihydrodipicolinate Synthase | |
| Identifiers | |
| Swiss Prot | |
| Genbank | |
| PDB | |
| Chemical data | |
| Formula | ? |
| Mol. wt. | 30,858 Da |
| Pharmacokinetic data | |
| Bioavailability | ? |
| Solubility | ? |
| Isoelectric-Point | 5.57 |
Contents |
General
dapA catalyzes the formation of dihydrodipicolinate from L-aspartate 4-semialdehyde and pyruvate.
L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2H2O.
This protein is eesential for optimal growth of M.tb and found in the cytoplasm as predicted by the WoLFPSORT and Subloc Server. HMMpfam found one domain PF00701 and has Helix Turn Helix secondary structure.
Amino Acid Sequence of Rv2753c
>Rv2753c, TB.seq 3066222:3067121 MW:30827 VTTVGFDVAARLGTLLTAMVTPFSGDGSLDTATAARLANHLVDQGCDGLVVSGTTGESPTTTDGEKIELLRAVLEAVGDR ARVIAGAGTYDTAHSIRLAKACAAEGAHGLLVVTPYYSKPPQRGLQAHFTAVADATELPMLLYDIPGRSAVPIEPDTIRA LASHPNIVGVKDAKADLHSGAQIMADTGLAYYSGDDALNLPWLAMGATGFISVIAHLAAGQLRELLSAFGSGDIATARKI NIAVAPLCNAMSRLGGVTLSKAGLRLQGIDVGDPRLPQVAATPEQIDALAADMRAASVLR
PDB Structure
This protein structure is available in PDB and having code 1XXX
Detail information available at OCA browser 1XXX
Discussion on this protein available at TopSCAN 1XXX
Structure Classification
Protein: Dihydrodipicolinate synthase from Mycobacterium tuberculosis SCOP_1XXX
Structural classification of 1XXX as per CATH CATH_1XXX
Human Homologue Blast Result
| subject ids | % identity | % positives | alignment length | evalue |
| sp|Q9BXD5 | 28 | 46.33 | 300 | 3.00E-023 |
| sp|Q86XE5 | 26.57 | 46.15 | 286 | 4.00E-022 |
| sp|Q9UG63 | 26.49 | 37.75 | 151 | 0.45 |
| sp|O14556 | 22.09 | 50 | 86 | 2 |
| sp|Q7Z7B0 | 27.69 | 44.62 | 65 | 2.7 |
Antigens
=Related Publications=
Crystal structure and kinetic study of dihydrodipicolinate synthase from Mycobacterium tuberculosis. Biochem J. 2008 Apr 15;411(2):351-60
Conserved main-chain peptide distortions: a proposed role for Ile203 in catalysis by dihydrodipicolinate synthase. Protein Sci. 2008 Dec;17(12):2080-90. Epub 2008 Sep 11
