1pm3

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(New page: 200px<br /><applet load="1pm3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pm3, resolution 3.15&Aring;" /> '''MTH1859'''<br /> ==...)
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[[Image:1pm3.gif|left|200px]]<br /><applet load="1pm3" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1pm3, resolution 3.15&Aring;" />
caption="1pm3, resolution 3.15&Aring;" />
'''MTH1859'''<br />
'''MTH1859'''<br />
==Overview==
==Overview==
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MTH1859 from Methanobacterium thermoautotrophicum is a 77 residue protein, representing a conserved family of functionally uncharacterized proteins., We solved the crystal structure of MTH1859 by single wavelength anomalous, diffraction phasing using selenomethionine labeled protein. MTH1859 adopts, a mainly anti-parallel all-beta-fold. The beta-sheet is heavily bent to, form a U-structure that is closed through a loop. The monomer structure, possesses similarities to the photoreaction center (PRC) domain fold, but, the protein employs a unique oligomerization scheme. Two monomers of, MTH1859 occupy the asymmetric unit and dimerize in a head-to-head fashion., Crystal packing interactions identify a second protein-protein interaction, interface at the MTH1859 tails which can simultaneously bind two partner, molecules. These interactions lead to the formation of a honeycomb, structure and suggest that the family of MTH1859-like proteins might, function as adapters for protein complex assembly.
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MTH1859 from Methanobacterium thermoautotrophicum is a 77 residue protein representing a conserved family of functionally uncharacterized proteins. We solved the crystal structure of MTH1859 by single wavelength anomalous diffraction phasing using selenomethionine labeled protein. MTH1859 adopts a mainly anti-parallel all-beta-fold. The beta-sheet is heavily bent to form a U-structure that is closed through a loop. The monomer structure possesses similarities to the photoreaction center (PRC) domain fold, but the protein employs a unique oligomerization scheme. Two monomers of MTH1859 occupy the asymmetric unit and dimerize in a head-to-head fashion. Crystal packing interactions identify a second protein-protein interaction interface at the MTH1859 tails which can simultaneously bind two partner molecules. These interactions lead to the formation of a honeycomb structure and suggest that the family of MTH1859-like proteins might function as adapters for protein complex assembly.
==About this Structure==
==About this Structure==
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1PM3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PM3 OCA].
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1PM3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PM3 OCA].
==Reference==
==Reference==
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[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: NESG, Northeast.Structural.Genomics.Consortium.]]
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[[Category: NESG, Northeast Structural Genomics Consortium.]]
[[Category: Steegborn, C.]]
[[Category: Steegborn, C.]]
[[Category: Wu, H.]]
[[Category: Wu, H.]]
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[[Category: unknown function]]
[[Category: unknown function]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:40:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:09 2008''

Revision as of 12:30, 21 February 2008


1pm3, resolution 3.15Å

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MTH1859

Overview

MTH1859 from Methanobacterium thermoautotrophicum is a 77 residue protein representing a conserved family of functionally uncharacterized proteins. We solved the crystal structure of MTH1859 by single wavelength anomalous diffraction phasing using selenomethionine labeled protein. MTH1859 adopts a mainly anti-parallel all-beta-fold. The beta-sheet is heavily bent to form a U-structure that is closed through a loop. The monomer structure possesses similarities to the photoreaction center (PRC) domain fold, but the protein employs a unique oligomerization scheme. Two monomers of MTH1859 occupy the asymmetric unit and dimerize in a head-to-head fashion. Crystal packing interactions identify a second protein-protein interaction interface at the MTH1859 tails which can simultaneously bind two partner molecules. These interactions lead to the formation of a honeycomb structure and suggest that the family of MTH1859-like proteins might function as adapters for protein complex assembly.

About this Structure

1PM3 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the putative adapter protein MTH1859., Ye H, Chen TC, Xu X, Pennycooke M, Wu H, Steegborn C, J Struct Biol. 2004 Nov;148(2):251-6. PMID:15477104

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