1s2p
From Proteopedia
(New page: 200px<br /><applet load="1s2p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s2p, resolution 1.30Å" /> '''The structure and re...) |
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| - | [[Image:1s2p.jpg|left|200px]]<br /><applet load="1s2p" size=" | + | [[Image:1s2p.jpg|left|200px]]<br /><applet load="1s2p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1s2p, resolution 1.30Å" /> | caption="1s2p, resolution 1.30Å" /> | ||
'''The structure and refinement of apocrustacyanin C2 to 1.3A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1'''<br /> | '''The structure and refinement of apocrustacyanin C2 to 1.3A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The blue carotenoprotein alpha-crustacyanin of Homarus gammarus lobster | + | The blue carotenoprotein alpha-crustacyanin of Homarus gammarus lobster carapace is comprised chemically of five 20 kDa subunits. Only two genes for the proteins have been isolated (J. B. C. Findlay, personal communication) and the five apoproteins fall into two sets of homologous proteins based on their chemical properties (CRTC, consisting of apoproteins C(1), C(2) and A(1), and CRTA, consisting of apoproteins A(2) and A(3)). The diffraction quality of apo C(2) has been improved from 2.2 to 1.3 A and its structure solved. The structure is compared with the A(1) and C(1) proteins determined at 1.4 A [Cianci et al. (2001), Acta Cryst. D57, 1219-1229] and 1.15 A, respectively [Gordon et al. (2001), Acta Cryst. D57, 1230-1237] and found to be very similar. Normalized B-factor difference plots per residue of different types were used to try to find chemically modified residues; none were found at these resolutions. It remains possible that the differences between the CRTC proteins result from differences in amidation. By comparison of a crystal grown with glycerol (studied at 1.6 A) and one grown without glycerol (studied at 1.3 A) it was seen that glycerol bound at the astaxanthin site. |
==About this Structure== | ==About this Structure== | ||
| - | 1S2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homarus_gammarus Homarus gammarus] with SO4 and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1S2P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homarus_gammarus Homarus gammarus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homarus gammarus]] | [[Category: Homarus gammarus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chayen, N | + | [[Category: Chayen, N E.]] |
[[Category: Cianci, M.]] | [[Category: Cianci, M.]] | ||
[[Category: Habash, J.]] | [[Category: Habash, J.]] | ||
| - | [[Category: Helliwell, J | + | [[Category: Helliwell, J R.]] |
| - | [[Category: NNeji, G | + | [[Category: NNeji, G A.]] |
[[Category: Raftery, J.]] | [[Category: Raftery, J.]] | ||
| - | [[Category: Rizkallah, P | + | [[Category: Rizkallah, P J.]] |
| - | [[Category: Zakalsky, P | + | [[Category: Zakalsky, P F.]] |
[[Category: MPD]] | [[Category: MPD]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: x-ray refinement]] | [[Category: x-ray refinement]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:24 2008'' |
Revision as of 12:57, 21 February 2008
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The structure and refinement of apocrustacyanin C2 to 1.3A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1
Overview
The blue carotenoprotein alpha-crustacyanin of Homarus gammarus lobster carapace is comprised chemically of five 20 kDa subunits. Only two genes for the proteins have been isolated (J. B. C. Findlay, personal communication) and the five apoproteins fall into two sets of homologous proteins based on their chemical properties (CRTC, consisting of apoproteins C(1), C(2) and A(1), and CRTA, consisting of apoproteins A(2) and A(3)). The diffraction quality of apo C(2) has been improved from 2.2 to 1.3 A and its structure solved. The structure is compared with the A(1) and C(1) proteins determined at 1.4 A [Cianci et al. (2001), Acta Cryst. D57, 1219-1229] and 1.15 A, respectively [Gordon et al. (2001), Acta Cryst. D57, 1230-1237] and found to be very similar. Normalized B-factor difference plots per residue of different types were used to try to find chemically modified residues; none were found at these resolutions. It remains possible that the differences between the CRTC proteins result from differences in amidation. By comparison of a crystal grown with glycerol (studied at 1.6 A) and one grown without glycerol (studied at 1.3 A) it was seen that glycerol bound at the astaxanthin site.
About this Structure
1S2P is a Single protein structure of sequence from Homarus gammarus with and as ligands. Full crystallographic information is available from OCA.
Reference
The structure and refinement of apocrustacyanin C2 to 1.3 A resolution and the search for differences between this protein and the homologous apoproteins A1 and C1., Habash J, Helliwell JR, Raftery J, Cianci M, Rizkallah PJ, Chayen NE, Nneji GA, Zagalsky PF, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):493-8. Epub 2004, Feb 25. PMID:14993674
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