1rb5

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(New page: 200px<br /><applet load="1rb5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rb5, resolution 1.9&Aring;" /> '''ANTIPARALLEL TRIMER O...)
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[[Image:1rb5.jpg|left|200px]]<br /><applet load="1rb5" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rb5.jpg|left|200px]]<br /><applet load="1rb5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rb5, resolution 1.9&Aring;" />
caption="1rb5, resolution 1.9&Aring;" />
'''ANTIPARALLEL TRIMER OF GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A TRIGONAL FORM'''<br />
'''ANTIPARALLEL TRIMER OF GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A TRIGONAL FORM'''<br />
==Overview==
==Overview==
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Efficient determination of protein crystal structures requires automated, x-ray data analysis. Here, we describe the expert system ELVES and its use, to determine automatically the structure of a 12-kDa protein., Multiwavelength anomalous diffraction analysis of a selenomethionyl, derivative was used to image the Asn-16-Ala variant of the GCN4 leucine, zipper. In contrast to the parallel, dimeric coiled coil formed by the WT, sequence, the mutant unexpectedly formed an antiparallel trimer. This, structural switch reveals how avoidance of core cavities at a single site, can select the native fold of a protein. All structure calculations, including indexing, data processing, locating heavy atoms, phasing by, multiwavelength anomalous diffraction, model building, and refinement, were completed without human intervention. The results demonstrate the, feasibility of automated methods for determining high-resolution, x-ray, crystal structures of proteins.
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Efficient determination of protein crystal structures requires automated x-ray data analysis. Here, we describe the expert system ELVES and its use to determine automatically the structure of a 12-kDa protein. Multiwavelength anomalous diffraction analysis of a selenomethionyl derivative was used to image the Asn-16-Ala variant of the GCN4 leucine zipper. In contrast to the parallel, dimeric coiled coil formed by the WT sequence, the mutant unexpectedly formed an antiparallel trimer. This structural switch reveals how avoidance of core cavities at a single site can select the native fold of a protein. All structure calculations, including indexing, data processing, locating heavy atoms, phasing by multiwavelength anomalous diffraction, model building, and refinement, were completed without human intervention. The results demonstrate the feasibility of automated methods for determining high-resolution, x-ray crystal structures of proteins.
==About this Structure==
==About this Structure==
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1RB5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RB5 OCA].
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1RB5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RB5 OCA].
==Reference==
==Reference==
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[[Category: peptide]]
[[Category: peptide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:25:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:48:59 2008''

Revision as of 12:48, 21 February 2008

Image:1rb5.jpg

1rb5, resolution 1.9Å

Drag the structure with the mouse to rotate

ANTIPARALLEL TRIMER OF GCN4-LEUCINE ZIPPER CORE MUTANT AS N16A TRIGONAL FORM

Overview

Efficient determination of protein crystal structures requires automated x-ray data analysis. Here, we describe the expert system ELVES and its use to determine automatically the structure of a 12-kDa protein. Multiwavelength anomalous diffraction analysis of a selenomethionyl derivative was used to image the Asn-16-Ala variant of the GCN4 leucine zipper. In contrast to the parallel, dimeric coiled coil formed by the WT sequence, the mutant unexpectedly formed an antiparallel trimer. This structural switch reveals how avoidance of core cavities at a single site can select the native fold of a protein. All structure calculations, including indexing, data processing, locating heavy atoms, phasing by multiwavelength anomalous diffraction, model building, and refinement, were completed without human intervention. The results demonstrate the feasibility of automated methods for determining high-resolution, x-ray crystal structures of proteins.

About this Structure

1RB5 is a Single protein structure of sequence from [1] with as ligand. Full crystallographic information is available from OCA.

Reference

Automated protein crystal structure determination using ELVES., Holton J, Alber T, Proc Natl Acad Sci U S A. 2004 Feb 10;101(6):1537-42. Epub 2004 Jan 29. PMID:14752198

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