1lfp

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(New page: 200px<br /><applet load="1lfp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lfp, resolution 1.72&Aring;" /> '''Crystal Structure of...)
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[[Image:1lfp.gif|left|200px]]<br /><applet load="1lfp" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lfp.gif|left|200px]]<br /><applet load="1lfp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lfp, resolution 1.72&Aring;" />
caption="1lfp, resolution 1.72&Aring;" />
'''Crystal Structure of a Conserved Hypothetical Protein Aq1575 from Aquifex Aeolicus'''<br />
'''Crystal Structure of a Conserved Hypothetical Protein Aq1575 from Aquifex Aeolicus'''<br />
==Overview==
==Overview==
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The crystal structure of a conserved hypothetical protein, Aq1575, from, Aquifex aeolicus has been determined by using x-ray crystallography. The, protein belongs to the domain of unknown function DUF28 in the Pfam and, PALI databases for which there was no structural information available, until now. A structural homology search with the DALI algorithm indicates, that this protein has a new fold with no obvious similarity to those of, other proteins of known three-dimensional structure. The protein reveals a, monomer consisting of three domains arranged along a pseudo threefold, symmetry axis. There is a large cleft with approximate dimensions of 10 A, x 10 A x 20 A in the center of the three domains along the symmetry axis., Two possible active sites are suggested based on the structure and, multiple sequence alignment. There are several highly conserved residues, in these putative active sites. The structure based molecular properties, and thermostability of the protein are discussed.
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The crystal structure of a conserved hypothetical protein, Aq1575, from Aquifex aeolicus has been determined by using x-ray crystallography. The protein belongs to the domain of unknown function DUF28 in the Pfam and PALI databases for which there was no structural information available until now. A structural homology search with the DALI algorithm indicates that this protein has a new fold with no obvious similarity to those of other proteins of known three-dimensional structure. The protein reveals a monomer consisting of three domains arranged along a pseudo threefold symmetry axis. There is a large cleft with approximate dimensions of 10 A x 10 A x 20 A in the center of the three domains along the symmetry axis. Two possible active sites are suggested based on the structure and multiple sequence alignment. There are several highly conserved residues in these putative active sites. The structure based molecular properties and thermostability of the protein are discussed.
==About this Structure==
==About this Structure==
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1LFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LFP OCA].
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1LFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LFP OCA].
==Reference==
==Reference==
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[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Kim, R.]]
[[Category: Kim, R.]]
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[[Category: Kim, S.H.]]
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[[Category: Kim, S H.]]
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[[Category: Shin, D.H.]]
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[[Category: Shin, D H.]]
[[Category: Yokota, H.]]
[[Category: Yokota, H.]]
[[Category: berkeley structural genomics center]]
[[Category: berkeley structural genomics center]]
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[[Category: thermostability]]
[[Category: thermostability]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:32:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:33 2008''

Revision as of 11:44, 21 February 2008


1lfp, resolution 1.72Å

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Crystal Structure of a Conserved Hypothetical Protein Aq1575 from Aquifex Aeolicus

Overview

The crystal structure of a conserved hypothetical protein, Aq1575, from Aquifex aeolicus has been determined by using x-ray crystallography. The protein belongs to the domain of unknown function DUF28 in the Pfam and PALI databases for which there was no structural information available until now. A structural homology search with the DALI algorithm indicates that this protein has a new fold with no obvious similarity to those of other proteins of known three-dimensional structure. The protein reveals a monomer consisting of three domains arranged along a pseudo threefold symmetry axis. There is a large cleft with approximate dimensions of 10 A x 10 A x 20 A in the center of the three domains along the symmetry axis. Two possible active sites are suggested based on the structure and multiple sequence alignment. There are several highly conserved residues in these putative active sites. The structure based molecular properties and thermostability of the protein are discussed.

About this Structure

1LFP is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of conserved hypothetical protein Aq1575 from Aquifex aeolicus., Shin DH, Yokota H, Kim R, Kim SH, Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):7980-5. PMID:12060744

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