1nmd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nmd.jpg|left|200px]]<br /><applet load="1nmd" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1nmd.jpg|left|200px]]
-
caption="1nmd, resolution 1.90&Aring;" />
+
 
-
'''Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP'''<br />
+
{{Structure
 +
|PDB= 1nmd |SIZE=350|CAPTION= <scene name='initialview01'>1nmd</scene>, resolution 1.90&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=SO2:SULFUR DIOXIDE'>SO2</scene>
 +
|ACTIVITY=
 +
|GENE= GSN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
}}
 +
 
 +
'''Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
1NMD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=SO2:'>SO2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMD OCA].
+
1NMD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMD OCA].
==Reference==
==Reference==
-
The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism., Vorobiev S, Strokopytov B, Drubin DG, Frieden C, Ono S, Condeelis J, Rubenstein PA, Almo SC, Proc Natl Acad Sci U S A. 2003 May 13;100(10):5760-5. Epub 2003 May 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12732734 12732734]
+
The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism., Vorobiev S, Strokopytov B, Drubin DG, Frieden C, Ono S, Condeelis J, Rubenstein PA, Almo SC, Proc Natl Acad Sci U S A. 2003 May 13;100(10):5760-5. Epub 2003 May 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12732734 12732734]
[[Category: Dictyostelium discoideum]]
[[Category: Dictyostelium discoideum]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 30: Line 39:
[[Category: gelsolin]]
[[Category: gelsolin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:36 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:58:44 2008''

Revision as of 10:58, 20 March 2008


PDB ID 1nmd

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: , , and
Gene: GSN (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP


Contents

Overview

The structures of Saccharomyces cerevisiae, Dictyostelium, and Caenorhabditis elegans actin bound to gelsolin segment-1 have been solved and refined at resolutions between 1.9 and 1.75 A. These structures reveal several features relevant to the ATP hydrolytic mechanism, including identification of the nucleophilic water and the roles of Gln-137 and His-161 in positioning and activating the catalytic water, respectively. The involvement of these residues in the catalytic mechanism is consistent with yeast genetics studies. This work highlights both structural and mechanistic similarities with the small and trimeric G proteins and restricts the types of mechanisms responsible for the considerable enhancement of ATP hydrolysis associated with actin polymerization. The conservation of functionalities involved in nucleotide binding and catalysis also provide insights into the mechanistic features of members of the family of actin-related proteins.

Disease

Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[137350]

About this Structure

1NMD is a Protein complex structure of sequences from Dictyostelium discoideum and Homo sapiens. Full crystallographic information is available from OCA.

Reference

The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism., Vorobiev S, Strokopytov B, Drubin DG, Frieden C, Ono S, Condeelis J, Rubenstein PA, Almo SC, Proc Natl Acad Sci U S A. 2003 May 13;100(10):5760-5. Epub 2003 May 5. PMID:12732734

Page seeded by OCA on Thu Mar 20 12:58:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools