1p8z
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1p8z |SIZE=350|CAPTION= <scene name='initialview01'>1p8z</scene>, resolution 2.60Å | |PDB= 1p8z |SIZE=350|CAPTION= <scene name='initialview01'>1p8z</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p8z OCA], [http://www.ebi.ac.uk/pdbsum/1p8z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p8z RCSB]</span> | ||
}} | }} | ||
| Line 14: | Line 17: | ||
==Overview== | ==Overview== | ||
We present the 2.6 A resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin. | We present the 2.6 A resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin. | ||
| - | |||
| - | ==Disease== | ||
| - | Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=137350 137350]] | ||
==About this Structure== | ==About this Structure== | ||
| Line 29: | Line 29: | ||
[[Category: Irobi, E.]] | [[Category: Irobi, E.]] | ||
[[Category: Robinson, R C.]] | [[Category: Robinson, R C.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CD]] | ||
[[Category: linker between gelsolin domain 1 and domain 2]] | [[Category: linker between gelsolin domain 1 and domain 2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:56:34 2008'' |
Revision as of 19:56, 30 March 2008
| |||||||
| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156
Overview
We present the 2.6 A resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-Gln160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin.
About this Structure
1P8Z is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
From the first to the second domain of gelsolin: a common path on the surface of actin?, Irobi E, Burtnick LD, Urosev D, Narayan K, Robinson RC, FEBS Lett. 2003 Sep 25;552(2-3):86-90. PMID:14527665
Page seeded by OCA on Sun Mar 30 22:56:34 2008
