+Open data
-Basic information
Entry | Database: PDB / ID: 2btf | ||||||
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Title | THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN | ||||||
Components |
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Keywords | ACETYLATION AND ACTIN-BINDING | ||||||
Function / homology | Function and homology information PCP/CE pathway / Adherens junctions interactions / Cell-extracellular matrix interactions / B-WICH complex positively regulates rRNA expression / Gap junction degradation / Formation of annular gap junctions / MAP2K and MAPK activation / RHOF GTPase cycle / EPHB-mediated forward signaling / Regulation of actin dynamics for phagocytic cup formation ...PCP/CE pathway / Adherens junctions interactions / Cell-extracellular matrix interactions / B-WICH complex positively regulates rRNA expression / Gap junction degradation / Formation of annular gap junctions / MAP2K and MAPK activation / RHOF GTPase cycle / EPHB-mediated forward signaling / Regulation of actin dynamics for phagocytic cup formation / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / DNA Damage Recognition in GG-NER / UCH proteinases / VEGFA-VEGFR2 Pathway / structural constituent of postsynaptic actin cytoskeleton / positive regulation of actin filament bundle assembly / dense body / regulation of actin filament polymerization / Clathrin-mediated endocytosis / NuA4 histone acetyltransferase complex / axonogenesis / actin filament / cell motility / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / actin cytoskeleton / actin binding / actin cytoskeleton organization / cytoskeleton / hydrolase activity / axon / focal adhesion / synapse / protein kinase binding / protein-containing complex / ATP binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.55 Å | ||||||
Authors | Schutt, C.E. / Myslik, J.C. / Rozycki, M.D. / Goonesekere, N.C.W. | ||||||
Citation | Journal: Nature / Year: 1993 Title: The structure of crystalline profilin-beta-actin. Authors: Schutt, C.E. / Myslik, J.C. / Rozycki, M.D. / Goonesekere, N.C. / Lindberg, U. #1: Journal: To be Published Title: Structural Aspects of Actin Binding Proteins Current Opinion in Cell Biology Authors: Rozycki, M.D. / Myslik, J.C. / Schutt, C.E. / Lindberg, U. #2: Journal: FEBS Lett. / Year: 1993 Title: Mutagenesis of Human Profilin Locates its Poly(L-Proline)-Binding Site to a Hydrophobic Patch of Aromatic Amino Acids Authors: Bjorkegren, C. / Rozycki, M. / Schutt, C.E. / Lindberg, U. / Karlsson, R. #3: Journal: J.Mol.Biol. / Year: 1989 Title: Molecular Packing in Profilin-Actin Crystals and its Implications Authors: Schutt, C.E. / Lindberg, U. / Myslik, J. / Strauss, N. | ||||||
History |
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Remark 650 | HELIX RESIDUES ARE INCLUDED AT THE BEGINNING OF HELICES IF THEY PARTICIPATE IN HYDROGEN BONDING AND ...HELIX RESIDUES ARE INCLUDED AT THE BEGINNING OF HELICES IF THEY PARTICIPATE IN HYDROGEN BONDING AND ARE "PARTIALLY" HELICAL, EVEN IF THE ENTIRE RESIDUE DOES NOT FIT HELICAL CRITERIA. | ||||||
Remark 700 | SHEET PROFILIN IS DESCRIBED IN JRNL REFERENCE AS HAVING A SIX-MEMBERED BETA-SHEET WHICH SHARES A ...SHEET PROFILIN IS DESCRIBED IN JRNL REFERENCE AS HAVING A SIX-MEMBERED BETA-SHEET WHICH SHARES A STRAND WITH A SECOND TWO-MEMBERED SHEET. TO CONFORM WITH PROTEIN DATA BANK GUIDELINES, THESE SHEETS ARE COMBINED INTO A SINGLE SEVEN-MEMBERED SHEET (SP1) IN THIS ENTRY. STRAND NUMBERING ALSO DIFFERS FROM THE JRNL REFERENCE. SECONDARY STRUCTURE ASSIGNMENTS FOR BETA-ACTIN ARE SIMILAR TO THOSE USED FOR ALPHA-ACTIN (PROTEIN DATA BANK ENTRY 1ATN) WITH MINOR CHANGES. HOWEVER, THE NOMENCLATURE USED HEREIN DIFFERS FROM THAT USED IN THE ABOVE ENTRY. ALSO, STRAND A4B DESCRIBED IN THAT ENTRY IS NOT INCLUDED HERE BECAUSE THE "ALTERNATIVE" STRAND TO ONE IN STRAND A4A (CORRESPONDING TO SA4 IN THIS ENTRY) IS ONLY TWO RESIDUES IN LENGTH. IN CONTRAST, SHEET SA3 IS INCLUDED BECAUSE IT CONTAINS TWO STRANDS AND A WELL-DEFINED TYPE II TURN, EVEN THOUGH THE TWO STRANDS CONTAIN ONLY TWO RESIDUES EACH. RESIDUE P 31 IS A BETA-BULGE. RESIDUE P 73 IS A BETA-BULGE, REDIRECTING STRAND 6. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2btf.cif.gz | 109.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2btf.ent.gz | 87.8 KB | Display | PDB format |
PDBx/mmJSON format | 2btf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2btf_validation.pdf.gz | 474 KB | Display | wwPDB validaton report |
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Full document | 2btf_full_validation.pdf.gz | 498.8 KB | Display | |
Data in XML | 2btf_validation.xml.gz | 15.1 KB | Display | |
Data in CIF | 2btf_validation.cif.gz | 21.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bt/2btf ftp://data.pdbj.org/pub/pdb/validation_reports/bt/2btf | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUE ACE A IS THE N-ACETYL MOIETY OF ACTIN. / 2: RESIDUE A 73 IS 3-METHYL HISTIDYL. / 3: RESIDUE ACE P IS THE N-ACETYL MOIETY OF PROFILIN. / 4: RESIDUE P 31 IS A BETA-BULGE. / 5: RESIDUE P 73 IS A BETA-BULGE, REDIRECTING STRAND 6. |
-Components
#1: Protein | Mass: 41690.520 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P60712 |
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#2: Protein | Mass: 14968.185 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / References: UniProt: P02584 |
#3: Chemical | ChemComp-SR / |
#4: Chemical | ChemComp-ATP / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.6 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging dropDetails: referred to 'Segura, M. & Lindberg, U.', (1984) J.Biol.Chem., 259, 3949-3954 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.55 Å / Num. obs: 16158 / % possible obs: 98.8 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.065 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.199 / Rfactor obs: 0.199 / Highest resolution: 2.55 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.55 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 8 Å / σ(F): 3 / Rfactor obs: 0.199 / Rfactor Rwork: 0.199 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 19.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 2.55 Å / Lowest resolution: 2.66 Å / Total num. of bins used: 8 / Num. reflection obs: 1539 / Rfactor obs: 0.2961 |