1s0p

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'''Structure of the N-Terminal Domain of the Adenylyl Cyclase-Associated Protein (CAP) from Dictyostelium discoideum.'''<br />
'''Structure of the N-Terminal Domain of the Adenylyl Cyclase-Associated Protein (CAP) from Dictyostelium discoideum.'''<br />
==Overview==
==Overview==
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Cyclase-associated proteins (CAPs) are widely distributed and highly, conserved proteins that regulate actin remodeling in response to cellular, signals. The N termini of CAPs play a role in Ras signaling and bind, adenylyl cyclase; the C termini bind to G-actin and thereby alter the, dynamic rearrangements of the microfilament system. We report here the, X-ray structure of the core of the N-terminal domain of the CAP from, Dictyostelium discoideum, which comprises residues 51-226, determined by a, combination of single isomorphous replacement with anomalous scattering, (SIRAS). The overall structure of this fragment is an alpha helix bundle, composed of six antiparallel helices. Results from gel filtration and, crosslinking experiments for CAP(1-226), CAP(255-464), and the full-length, protein, together with the CAP N-terminal domain structure and the, recently determined CAP C-terminal domain structure, provide evidence that, the functional structure of CAP is multimeric.
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Cyclase-associated proteins (CAPs) are widely distributed and highly conserved proteins that regulate actin remodeling in response to cellular signals. The N termini of CAPs play a role in Ras signaling and bind adenylyl cyclase; the C termini bind to G-actin and thereby alter the dynamic rearrangements of the microfilament system. We report here the X-ray structure of the core of the N-terminal domain of the CAP from Dictyostelium discoideum, which comprises residues 51-226, determined by a combination of single isomorphous replacement with anomalous scattering (SIRAS). The overall structure of this fragment is an alpha helix bundle composed of six antiparallel helices. Results from gel filtration and crosslinking experiments for CAP(1-226), CAP(255-464), and the full-length protein, together with the CAP N-terminal domain structure and the recently determined CAP C-terminal domain structure, provide evidence that the functional structure of CAP is multimeric.
==About this Structure==
==About this Structure==
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1S0P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. This structure superseeds the now removed PDB entry 1PN1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S0P OCA].
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1S0P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1PN1. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S0P OCA].
==Reference==
==Reference==
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[[Category: Dictyostelium discoideum]]
[[Category: Dictyostelium discoideum]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bartunik, H.D.]]
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[[Category: Bartunik, H D.]]
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[[Category: Bourenkov, G.P.]]
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[[Category: Bourenkov, G P.]]
[[Category: Brandstetter, H.]]
[[Category: Brandstetter, H.]]
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[[Category: Holak, T.A.]]
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[[Category: Holak, T A.]]
[[Category: Israel, L.]]
[[Category: Israel, L.]]
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[[Category: Janssen, K.P.]]
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[[Category: Janssen, K P.]]
[[Category: Katchalova, G.]]
[[Category: Katchalova, G.]]
[[Category: Ksiazek, D.]]
[[Category: Ksiazek, D.]]
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[[Category: Noegel, A.A.]]
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[[Category: Noegel, A A.]]
[[Category: Schleicher, M.]]
[[Category: Schleicher, M.]]
[[Category: MG]]
[[Category: MG]]
[[Category: alpha helix bundle]]
[[Category: alpha helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:01:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:42 2008''

Revision as of 12:56, 21 February 2008


1s0p, resolution 1.4Å

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Structure of the N-Terminal Domain of the Adenylyl Cyclase-Associated Protein (CAP) from Dictyostelium discoideum.

Overview

Cyclase-associated proteins (CAPs) are widely distributed and highly conserved proteins that regulate actin remodeling in response to cellular signals. The N termini of CAPs play a role in Ras signaling and bind adenylyl cyclase; the C termini bind to G-actin and thereby alter the dynamic rearrangements of the microfilament system. We report here the X-ray structure of the core of the N-terminal domain of the CAP from Dictyostelium discoideum, which comprises residues 51-226, determined by a combination of single isomorphous replacement with anomalous scattering (SIRAS). The overall structure of this fragment is an alpha helix bundle composed of six antiparallel helices. Results from gel filtration and crosslinking experiments for CAP(1-226), CAP(255-464), and the full-length protein, together with the CAP N-terminal domain structure and the recently determined CAP C-terminal domain structure, provide evidence that the functional structure of CAP is multimeric.

About this Structure

1S0P is a Single protein structure of sequence from Dictyostelium discoideum with as ligand. This structure supersedes the now removed PDB entry 1PN1. Full crystallographic information is available from OCA.

Reference

Structure of the N-terminal domain of the adenylyl cyclase-associated protein (CAP) from Dictyostelium discoideum., Ksiazek D, Brandstetter H, Israel L, Bourenkov GP, Katchalova G, Janssen KP, Bartunik HD, Noegel AA, Schleicher M, Holak TA, Structure. 2003 Sep;11(9):1171-8. PMID:12962635

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