1aux: Difference between revisions

← Older edit Newer edit →

Revision as of 11:02, 20 March 2008

File:1aux.gif

, resolution 2.30Å

Ligands:

and

Coordinates:

save as pdb, mmCIF, xml

STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND

OverviewOverview

Synapsins are abundant synaptic vesicle proteins with an essential regulatory function in the nerve terminal. We determined the crystal structure of a fragment (synC) consisting of residues 110-420 of bovine synapsin I; synC coincides with the large middle domain (C-domain), the most conserved domain of synapsins. SynC molecules are folded into compact domains and form closely associated dimers. SynC monomers are strikingly similar in structure to a family of ATP-utilizing enzymes, which includes glutathione synthetase and D-alanine:D-alanine ligase. SynC binds ATP in a Ca2+-dependent manner. The crystal structure of synC in complex with ATPgammaS and Ca2+ explains the preference of synC for Ca2+ over Mg2+. Our results suggest that synapsins may also be ATP-utilizing enzymes.

About this StructureAbout this Structure

1AUX is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Synapsin I is structurally similar to ATP-utilizing enzymes., Esser L, Wang CR, Hosaka M, Smagula CS, Sudhof TC, Deisenhofer J, EMBO J. 1998 Feb 16;17(4):977-84. PMID:9463376

Page seeded by OCA on Thu Mar 20 10:02:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1aux.gif|left|200px]]<br /><applet load="1aux" size="350" color="white" frame="true" align="right" spinBox="true"
+[[Image:1aux.gif|left|200px]]
-caption="1aux, resolution 2.30&Aring;" />
-'''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND'''<br />
+ {{Structure
+|PDB= 1aux |SIZE=350|CAPTION= <scene name='initialview01'>1aux</scene>, resolution 2.30&Aring;
+|SITE=
+|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SAP:ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE'>SAP</scene>
+|ACTIVITY=
+|GENE=
+}}
+'''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND'''
 ==Overview==
@@ Line 7: / Line 16: @@
 ==About this Structure==
-AUX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SAP:'>SAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUX OCA].
+AUX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUX OCA].
 ==Reference==
-Synapsin I is structurally similar to ATP-utilizing enzymes., Esser L, Wang CR, Hosaka M, Smagula CS, Sudhof TC, Deisenhofer J, EMBO J. 1998 Feb 16;17(4):977-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9463376 9463376]
+Synapsin I is structurally similar to ATP-utilizing enzymes., Esser L, Wang CR, Hosaka M, Smagula CS, Sudhof TC, Deisenhofer J, EMBO J. 1998 Feb 16;17(4):977-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9463376 9463376]
 [[Category: Bos taurus]]
 [[Category: Single protein]]
@@ Line 24: / Line 33: @@
 [[Category: synapsin ia c-domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:31 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:34 2008''