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Structure paper

TitleHow Leiomodin and Tropomodulin use a common fold for different actin assembly functions.
Journal, issue, pagesNat Commun, Vol. 6, Page 8314-8314, Year 2015
Publish dateApr 6, 2015 (structure data deposition date)
AuthorsBoczkowska, M. / Rebowski, G. / Kremneva, E. / Lappalainen, P. / Dominguez, R.
External linksNat Commun / PubMed:26370058
MethodsX-ray diffraction
Resolution1.54 - 2.4 Å
Structure data

PDB-4z79:
Leiomodin-1 Actin-Binding Site 2 (ABS2)
Method: X-RAY DIFFRACTION / Resolution: 1.54 Å

PDB-4z8g:
Chimera of Tropomodulin-1 and Leiomodin-1 Actin-Binding Site 2 (TL1 ABS2)
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-4z94:
Actin Complex With a Chimera of Tropomodulin-1 and Leiomodin-1 Actin-Binding Site 2
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-NI:
NICKEL (II) ION

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
  • oryctolagus cuniculus (rabbit)
KeywordsPROTEIN BINDING / Leiomodin-1 Actin Binding Site 2 ABS2 Actin nucleator / Actin Nucleator / Leucine Rich Repeat Domain / PROTEIN BINDING/STRUCTURAL PROTEIN / ATP-actin / PROTEIN BINDING-STRUCTURAL PROTEIN complex

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