RSP1275
Background InformationBackground Information
Rsp1275 is a member of the Fnr-Crp family of transcriptional regulators. Homologues of the Fnr protein from E. coli have been identified in a variety of taxonomically diverse bacterial species.[1][2]The bacterium Rhodobacter sphaeroides" 2.4.1 encodes 8 members of this family, however only 2 have known function. Models of 7 of them, including RSP1275, were successfully obtained using 3D-Jigsaw, all being very similar in structure to Crp (the only one with crystal structure solved). The DNA binding domain helix-turn-helix is located in the C-terminal, and the N-terminal part contains the allosteric effector domain.
Structure of the Proposed rsp1275 modeling obtained using 3D-JigsawStructure of the Proposed rsp1275 modeling obtained using 3D-Jigsaw
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The highlighted of the protein.
This is the of the protein.
Protein SequenceProtein Sequence
1 mfvpapdati tncrncplrr kplflpfsds elsfmeqfkv gelvvapgvt lleegqgsah
61 lftvlsglgi rstmlengrr qvinflfpgd figlqaglag emrhsvestt tmvlcvfnra
121 dlwdlfreep eraydltwia aveehflget iaslgqrdat erlawallri herlsaigla
181 ergrvpmpwr qqdladalgl slvhtnktir rlretghalw eggtlfvdre rlatlaladp
241 drprrrpli
Physico - Chemical parameters for Rsp1275Physico - Chemical parameters for Rsp1275
From http://ca.expasy.org/tools/protparam.html
Number of amino acids: 249
Molecular weight: 28014.2
Theoretical pI: 6.10
Atomic composition:
Carbon C 1249 Hydrogen H 1986 Nitrogen N 360 Oxygen O 355 Sulfur S 9
Formula: C1249H1986N360O355S9 Total number of atoms: 3959
Extinction coefficients:
Extinction coefficients are in units of M-1 cm-1, at 280 nm measured in water.
- Ext. coefficient 29115
Abs 0.1% (=1 g/l) 1.039, assuming ALL Cys residues appear as half cystines
- Ext. coefficient 28990
Abs 0.1% (=1 g/l) 1.035, assuming NO Cys residues appear as half cystines
Estimated half-life:
The N-terminal of the sequence considered is M (Met).
The estimated half-life is:
- 30 hours (mammalian reticulocytes, in vitro).
- >20 hours (yeast, in vivo).
- >10 hours (Escherichia coli, in vivo).
Instability index:
The instability index (II) is computed to be 41.06 This classifies the protein as unstable.
Aliphatic index: 97.19
Grand average of hydropathicity (GRAVY): -0.097
Globe Prediction: it appears as compact, as a globular domain.
Secondary Structure: Helix 34.94% Extended (sheet) 17.67% Loop 47.39%
| Amino Acid | Number present | Percentage of total present |
|---|---|---|
| Ala (A) | 15 | 8.8% |
| Arg (R) | 10 | 10.4% |
| Asn (N) | 6 | 2.4% |
| Asp (D) | 10 | 4.8% |
| Cys (C) | 1 | 1.2% |
| Gln (Q) | 5 | 2.8% |
| Glu (E) | 11 | 8.0% |
| Gly (G) | 9 | 7.6% |
| His (H) | 10 | 2.4% |
| Ile (I) | 3 | 4.0% |
| Leu (L) | 21 | 14.5% |
| Lys (K) | 6 | 1.2% |
| Met (M) | 6 | 2.4% |
| Phe (F) | 2 | 4.0% |
| Pro (P) | 8 | 5.2% |
| Ser (S) | 7 | 4.4% |
| Thr (T) | 13 | 6.4% |
| Trp (W) | 2 | 2.0% |
| Tyr (Y) | 6 | 0.4% |
| Val (V) | 12 | 5.6% |
| Pyl (O) | 0 | 0.% |
| Sec (U) | 0 | 0.0% |
ReferenceReference
Page Created by Susana Retamal, email:susana.retamal@gmail.com
Acknownledment: Jill Zeilstra Ryalls, Adam Meade and Yana Fedotova.