2c4b

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[[Image:2c4b.gif|left|200px]]<br /><applet load="2c4b" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c4b.gif|left|200px]]<br /><applet load="2c4b" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2c4b, resolution 1.30&Aring;" />
caption="2c4b, resolution 1.30&Aring;" />
'''INHIBITOR CYSTINE KNOT PROTEIN MCOEETI FUSED TO THE CATALYTICALLY INACTIVE BARNASE MUTANT H102A'''<br />
'''INHIBITOR CYSTINE KNOT PROTEIN MCOEETI FUSED TO THE CATALYTICALLY INACTIVE BARNASE MUTANT H102A'''<br />
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==About this Structure==
==About this Structure==
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2C4B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens,_momordica_cochinchinensis,_ecballium_elaterium Bacillus amyloliquefaciens, momordica cochinchinensis, ecballium elaterium] with SO4, 2PE, EDO, MES, UNX, GOL and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Known structural/functional Site: <scene name='pdbsite=AC1:So4 Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C4B OCA].
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2C4B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens,_momordica_cochinchinensis,_ecballium_elaterium Bacillus amyloliquefaciens, momordica cochinchinensis, ecballium elaterium] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=2PE:'>2PE</scene>, <scene name='pdbligand=EDO:'>EDO</scene>, <scene name='pdbligand=MES:'>MES</scene>, <scene name='pdbligand=UNX:'>UNX</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] Known structural/functional Site: <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C4B OCA].
==Reference==
==Reference==
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[[Category: squash inhibitor]]
[[Category: squash inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:09:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:31:17 2008''

Revision as of 08:31, 3 February 2008


2c4b, resolution 1.30Å

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INHIBITOR CYSTINE KNOT PROTEIN MCOEETI FUSED TO THE CATALYTICALLY INACTIVE BARNASE MUTANT H102A

Overview

We present a fusion system suited to determine the crystal structure of, small disulfide-rich proteins. McoEeTI, a hybrid inhibitor cystine knot, microprotein, was produced as a soluble fusion to a catalytically inactive, variant of the RNAse barnase in Escherichia coli. Functioning as a, versatile tag, barnase facilitated purification, crystallization and, high-resolution structure determination. Flexibility of the linker region, allows for different relative orientations of barnase and the fusion, partner in two crystallographically independent molecules and may thereby, facilitate crystal packing. Nevertheless, the linker region is well, ordered in both molecules. This system may prove more generally useful to, determine the crystal structure of peptides and small proteins.

About this Structure

2C4B is a Single protein structure of sequence from Bacillus amyloliquefaciens, momordica cochinchinensis, ecballium elaterium with , , , , , and as ligands. Active as Ribonuclease T(1), with EC number 3.1.27.3 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI., Niemann HH, Schmoldt HU, Wentzel A, Kolmar H, Heinz DW, J Mol Biol. 2006 Feb 10;356(1):1-8. Epub 2005 Nov 21. PMID:16337652

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