2dma

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[[Image:2dma.gif|left|200px]]<br /><applet load="2dma" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2dma.gif|left|200px]]
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caption="2dma, resolution 2.05&Aring;" />
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'''Crystal Structure of PH1978 from Pyrococcus horikoshii OT3 (form II)'''<br />
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{{Structure
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|PDB= 2dma |SIZE=350|CAPTION= <scene name='initialview01'>2dma</scene>, resolution 2.05&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14]
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|GENE= atpE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=53953 Pyrococcus horikoshii])
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}}
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'''Crystal Structure of PH1978 from Pyrococcus horikoshii OT3 (form II)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2DMA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DMA OCA].
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2DMA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DMA OCA].
==Reference==
==Reference==
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Dimeric core structure of modular stator subunit E of archaeal H+ -ATPase., Lokanath NK, Matsuura Y, Kuroishi C, Takahashi N, Kunishima N, J Mol Biol. 2007 Feb 23;366(3):933-44. Epub 2006 Dec 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17189637 17189637]
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Dimeric core structure of modular stator subunit E of archaeal H+ -ATPase., Lokanath NK, Matsuura Y, Kuroishi C, Takahashi N, Kunishima N, J Mol Biol. 2007 Feb 23;366(3):933-44. Epub 2006 Dec 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17189637 17189637]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: Pyrococcus horikoshii]]
[[Category: Pyrococcus horikoshii]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: a-atpase]]
[[Category: a-atpase]]
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[[Category: national project on protein structural and functional analyses]]
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[[Category: national project on protein structural and functional analyse]]
[[Category: nppsfa]]
[[Category: nppsfa]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:00:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:28:51 2008''

Revision as of 14:28, 20 March 2008


PDB ID 2dma

Drag the structure with the mouse to rotate
, resolution 2.05Å
Gene: atpE (Pyrococcus horikoshii)
Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of PH1978 from Pyrococcus horikoshii OT3 (form II)


Overview

Archaeal H(+)-ATPase (A-ATPase) is composed of an A(1) region that hydrolyzes ATP and an integral membrane part A(0) that conducts protons. Subunit E is a component of peripheral stator(s) that physically links A(1) and A(0) parts of the A-ATPase. Here we report the first crystal structure of subunit E of A-ATPase from Pyrococcus horikoshii OT3 at 1.85 A resolution. The protomer structure of subunit E represents a novel fold. The quaternary structure of subunit E is a homodimer, which may constitute the core part of the stator. To investigate the relationship with other stator subunit H, the complex of subunits EH was prepared and characterized using electrophoresis, mass spectrometry, N-terminal sequencing and circular dichroism spectroscopy, which revealed the polymeric and highly helical nature of the EH complex with equimolar stoichiometry of both the subunits. On the basis of the modular architecture of stator subunits, it is suggested that both cytoplasm and membrane sides of the EH complex may interact with other subunits to link A(1) and A(0) parts.

About this Structure

2DMA is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.

Reference

Dimeric core structure of modular stator subunit E of archaeal H+ -ATPase., Lokanath NK, Matsuura Y, Kuroishi C, Takahashi N, Kunishima N, J Mol Biol. 2007 Feb 23;366(3):933-44. Epub 2006 Dec 9. PMID:17189637

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