+
Open data
-
Basic information
Entry | Database: PDB / ID: 1g6q | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF YEAST ARGININE METHYLTRANSFERASE, HMT1 | ||||||
![]() | HNRNP ARGININE N-METHYLTRANSFERASE | ||||||
![]() | TRANSFERASE / SAM-binding domain / beta-barrel / mixed alpha-beta / hexamer / dimer | ||||||
Function / homology | ![]() negative regulation of termination of DNA-templated transcription / protein-arginine omega-N monomethyltransferase activity / peptidyl-arginine methylation / protein-arginine omega-N asymmetric methyltransferase activity / folic acid biosynthetic process / RMTs methylate histone arginines / Estrogen-dependent gene expression / mRNA export from nucleus / Transferases; Transferring one-carbon groups; Methyltransferases / positive regulation of transcription elongation by RNA polymerase II ...negative regulation of termination of DNA-templated transcription / protein-arginine omega-N monomethyltransferase activity / peptidyl-arginine methylation / protein-arginine omega-N asymmetric methyltransferase activity / folic acid biosynthetic process / RMTs methylate histone arginines / Estrogen-dependent gene expression / mRNA export from nucleus / Transferases; Transferring one-carbon groups; Methyltransferases / positive regulation of transcription elongation by RNA polymerase II / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Weiss, V.H. / McBride, A.E. / Soriano, M.A. / Filman, D.J. / Silver, P.A. / Hogle, J.M. | ||||||
![]() | ![]() Title: The structure and oligomerization of the yeast arginine methyltransferase, Hmt1. Authors: Weiss, V.H. / McBride, A.E. / Soriano, M.A. / Filman, D.J. / Silver, P.A. / Hogle, J.M. #1: ![]() Title: Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions. Authors: McBride, A.E. / Weiss, V.H. / Kim, H.K. / Hogle, J.M. / Silver, P.A. #2: ![]() Title: Arginine methylation and binding of Hrp1p to the efficiency element for mRNA 3'-end formation. Authors: valentini, s.r. / weiss, v.h. / silver, p.a. #3: ![]() Title: A novel methyltransferase (Hmt1p) modifies poly(A)+RNA binding proteins. Authors: henry, m.f. / silver, p.a. #4: ![]() Title: Arginine methylation facilitates the nuclear export of hnRNP proteins. Authors: shen, e.c. / Henry, M.F. / Weiss, V.H. / Valentini, S.R. / Silver, P.A. / Lee, M.S. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 348.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 290.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 406.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 454.2 KB | Display | |
Data in XML | ![]() | 41.4 KB | Display | |
Data in CIF | ![]() | 61.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
4 | ![]()
| ||||||||
Unit cell |
| ||||||||
Details | hexamer has very approximate 32 symmetry. Monomers exhibit varying degrees of order. |
-
Components
#1: Protein | Mass: 37692.613 Da / Num. of mol.: 6 / Fragment: MISSING 20 AMINOACYL RESIDUES FROM N-TERMINUS / Mutation: Q21D, H22Y, N25D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: HMT1 Plasmid details: MODIFIED PET15B VECTOR CONTAINING INSERT PRECISSION PROTEASE SITE AFTER HIS TAG (PPS2193) Plasmid: PPS2193 / Production host: ![]() ![]() References: UniProt: P38074, Transferases; Transferring one-carbon groups; Methyltransferases |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.32 % | ||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 2 microliters of Hmt1 (8mg/ml) in 50 mM Tris, pH 7.0, 50 mM NaCl, 1 mM EDTA, 1 mM DTT + 2 microliters of reservoir:50 mM sodium hepes, pH 7.5, 14% v/v PEG 400, 100 mM CaCl2 + microseeds in 1 ...Details: 2 microliters of Hmt1 (8mg/ml) in 50 mM Tris, pH 7.0, 50 mM NaCl, 1 mM EDTA, 1 mM DTT + 2 microliters of reservoir:50 mM sodium hepes, pH 7.5, 14% v/v PEG 400, 100 mM CaCl2 + microseeds in 1 microliter of 20 mM sodium citrate, pH 5.6, 15% w/v PEG 4000, 100 mM ammonium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 22K | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 113 K | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||
Detector | Type: BRANDEIS / Detector: CCD / Date: Mar 2, 2000 / Details: monochromator | |||||||||||||||
Radiation | Monochromator: pair of parallel silicon crystals / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
| |||||||||||||||
Reflection | Resolution: 2.9→28 Å / Num. all: 91268 / Num. obs: 90403 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Biso Wilson estimate: 56.6 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 17.4 | |||||||||||||||
Reflection shell | Resolution: 2.89→2.99 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.235 / Mean I/σ(I) obs: 5 / Num. unique all: 8739 / Rsym value: 0.235 / % possible all: 95.9 | |||||||||||||||
Reflection | *PLUS Num. measured all: 277416 | |||||||||||||||
Reflection shell | *PLUS % possible obs: 95.9 % |
-
Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Details: 65 overlapping resolution-dependent bin scales, plus 1 or 2 grouped B values per aminoacyl residue. With bin-scales present, the refined B's do not correspond to rms displacements. NCS ...Details: 65 overlapping resolution-dependent bin scales, plus 1 or 2 grouped B values per aminoacyl residue. With bin-scales present, the refined B's do not correspond to rms displacements. NCS restraints were applied separately to the SAM-binding domains and the beta-barrel domains, with structurally variable segments of the polypeptide excluded.
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→28 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
LS refinement shell | Resolution: 2.9→2.97 Å /
| |||||||||||||||||||||||||
Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
|