1auv

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[[Image:1auv.gif|left|200px]]<br /><applet load="1auv" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1auv.gif|left|200px]]
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caption="1auv, resolution 2.15&Aring;" />
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'''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN'''<br />
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{{Structure
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|PDB= 1auv |SIZE=350|CAPTION= <scene name='initialview01'>1auv</scene>, resolution 2.15&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1AUV is a [http://en.wikipedia.org/wiki/Single_protein 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=1AUV OCA].
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1AUV 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=1AUV OCA].
==Reference==
==Reference==
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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]
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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: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: synapsin ia c-domain]]
[[Category: synapsin ia c-domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:33 2008''

Revision as of 08:02, 20 March 2008


PDB ID 1auv

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, resolution 2.15Å
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN


Overview

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 Structure

1AUV is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from 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:9463376

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