1noa
From Proteopedia
(New page: 200px<br /><applet load="1noa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1noa, resolution 1.5Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1noa.gif|left|200px]]<br /><applet load="1noa" size=" | + | [[Image:1noa.gif|left|200px]]<br /><applet load="1noa" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1noa, resolution 1.5Å" /> | caption="1noa, resolution 1.5Å" /> | ||
'''CRYSTAL STRUCTURE OF APO-NEOCARZINOSTATIN AT 0.15 NM RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF APO-NEOCARZINOSTATIN AT 0.15 NM RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of apo-neocarzinostatin, an antitumour | + | The three-dimensional structure of apo-neocarzinostatin, an antitumour antibiotic protein isolated from Streptomyces carzinostaticus, has been determined by X-ray diffraction at 0.15-nm resolution and refined to R = 17.2%. The crystal structure of neocarzinostatin is similar to that of the related proteins actinoxanthin and macromomycin. It is also in good agreement with the solution structure determined by NMR spectroscopy. The protein molecule consists of a seven-stranded antiparallel beta-sandwich and a smaller lobe formed by two beta-ribbons. A deep cleft between the two lobes is a putative chromophore binding site. Side chains of Trp39, Leu45, Phe52, Phe78 and the disulphide Cys37-Cys47 aligning the binding cleft in neocarzinostatin suggest the importance of hydrophobic interactions in stabilizing the chromophore molecule. Comparison of the atomic models of neocarzinostatin, actinoxanthin and macromomycin reveals functional residues which might determine specificity towards different chromophores. |
==About this Structure== | ==About this Structure== | ||
| - | 1NOA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_carzinostaticus Streptomyces carzinostaticus]. Full crystallographic information is available from [http:// | + | 1NOA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_carzinostaticus Streptomyces carzinostaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: antibacterial protein]] | [[Category: antibacterial protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:15 2008'' |
Revision as of 12:08, 21 February 2008
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CRYSTAL STRUCTURE OF APO-NEOCARZINOSTATIN AT 0.15 NM RESOLUTION
Overview
The three-dimensional structure of apo-neocarzinostatin, an antitumour antibiotic protein isolated from Streptomyces carzinostaticus, has been determined by X-ray diffraction at 0.15-nm resolution and refined to R = 17.2%. The crystal structure of neocarzinostatin is similar to that of the related proteins actinoxanthin and macromomycin. It is also in good agreement with the solution structure determined by NMR spectroscopy. The protein molecule consists of a seven-stranded antiparallel beta-sandwich and a smaller lobe formed by two beta-ribbons. A deep cleft between the two lobes is a putative chromophore binding site. Side chains of Trp39, Leu45, Phe52, Phe78 and the disulphide Cys37-Cys47 aligning the binding cleft in neocarzinostatin suggest the importance of hydrophobic interactions in stabilizing the chromophore molecule. Comparison of the atomic models of neocarzinostatin, actinoxanthin and macromomycin reveals functional residues which might determine specificity towards different chromophores.
About this Structure
1NOA is a Single protein structure of sequence from Streptomyces carzinostaticus. Full crystallographic information is available from OCA.
Reference
Crystal structure of apo-neocarzinostatin at 0.15-nm resolution., Teplyakov A, Obmolova G, Wilson K, Kuromizu K, Eur J Biochem. 1993 Apr 15;213(2):737-41. PMID:8477746
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