1b3i
From Proteopedia
(New page: 200px<br /><applet load="1b3i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b3i" /> '''NMR SOLUTION STRUCTURE OF PLASTOCYANIN FROM ...) |
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| - | [[Image:1b3i.jpg|left|200px]]<br /><applet load="1b3i" size=" | + | [[Image:1b3i.jpg|left|200px]]<br /><applet load="1b3i" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR SOLUTION STRUCTURE OF PLASTOCYANIN FROM THE PHOTOSYNTHETIC PROKARYOTE, PROCHLOROTHRIX HOLLANDICA (MINIMIZED AVERAGE STRUCTURE)'''<br /> | '''NMR SOLUTION STRUCTURE OF PLASTOCYANIN FROM THE PHOTOSYNTHETIC PROKARYOTE, PROCHLOROTHRIX HOLLANDICA (MINIMIZED AVERAGE STRUCTURE)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of a divergent plastocyanin (PC) from the | + | The solution structure of a divergent plastocyanin (PC) from the photosynthetic prokaryote Prochlorothrix hollandica was determined by homonuclear 1H NMR spectroscopy. Nineteen structures were calculated from 1222 distance restraints, yielding a family of structures having an average rmsd of 0.42 +/- 0.08 A for backbone atoms and 0.71 +/- 0.07 A for heavy atoms to the mean structure. No distance constraint was violated by more than 0.26 A in the structure family. Despite the low number of conserved residues shared with other PC homologues, the overall folding pattern of P. hollandica PC is similar to other PCs, in that the protein forms a two-sheet beta-barrel tertiary structure. The greatest variability among the backbone structures is seen in the loop region from residues 47-60. The differences seen in the P. hollandica PC homologue likely arise due to a small deletion of 2-4 residues compared to the PC consensus; this yields a less extended loop containing a short alpha-helix from residues Ala52-Leu55. Additionally, the protein has an altered hydrophobic patch thought to be important in binding reaction partners. Whereas the backbone structure is very similar within the loops of the hydrophobic region, the presence of two unique residues (Tyr12 and Pro14) yields a structurally different hydrophobic surface likely important in binding P. hollandica Photosystem I. |
==About this Structure== | ==About this Structure== | ||
| - | 1B3I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Prochlorothrix_hollandica Prochlorothrix hollandica] with CU1 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Plastoquinol--plastocyanin_reductase Plastoquinol--plastocyanin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.99.1 1.10.99.1] Full crystallographic information is available from [http:// | + | 1B3I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Prochlorothrix_hollandica Prochlorothrix hollandica] with <scene name='pdbligand=CU1:'>CU1</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Plastoquinol--plastocyanin_reductase Plastoquinol--plastocyanin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.99.1 1.10.99.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B3I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Prochlorothrix hollandica]] | [[Category: Prochlorothrix hollandica]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Babu, C | + | [[Category: Babu, C R.]] |
| - | [[Category: Bullerjahn, G | + | [[Category: Bullerjahn, G S.]] |
| - | [[Category: Volkman, B | + | [[Category: Volkman, B F.]] |
[[Category: CU1]] | [[Category: CU1]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
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[[Category: type i copper protein]] | [[Category: type i copper protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:03 2008'' |
Revision as of 09:51, 21 February 2008
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NMR SOLUTION STRUCTURE OF PLASTOCYANIN FROM THE PHOTOSYNTHETIC PROKARYOTE, PROCHLOROTHRIX HOLLANDICA (MINIMIZED AVERAGE STRUCTURE)
Overview
The solution structure of a divergent plastocyanin (PC) from the photosynthetic prokaryote Prochlorothrix hollandica was determined by homonuclear 1H NMR spectroscopy. Nineteen structures were calculated from 1222 distance restraints, yielding a family of structures having an average rmsd of 0.42 +/- 0.08 A for backbone atoms and 0.71 +/- 0.07 A for heavy atoms to the mean structure. No distance constraint was violated by more than 0.26 A in the structure family. Despite the low number of conserved residues shared with other PC homologues, the overall folding pattern of P. hollandica PC is similar to other PCs, in that the protein forms a two-sheet beta-barrel tertiary structure. The greatest variability among the backbone structures is seen in the loop region from residues 47-60. The differences seen in the P. hollandica PC homologue likely arise due to a small deletion of 2-4 residues compared to the PC consensus; this yields a less extended loop containing a short alpha-helix from residues Ala52-Leu55. Additionally, the protein has an altered hydrophobic patch thought to be important in binding reaction partners. Whereas the backbone structure is very similar within the loops of the hydrophobic region, the presence of two unique residues (Tyr12 and Pro14) yields a structurally different hydrophobic surface likely important in binding P. hollandica Photosystem I.
About this Structure
1B3I is a Single protein structure of sequence from Prochlorothrix hollandica with as ligand. Active as Plastoquinol--plastocyanin reductase, with EC number 1.10.99.1 Full crystallographic information is available from OCA.
Reference
NMR solution structure of plastocyanin from the photosynthetic prokaryote, Prochlorothrix hollandica., Babu CR, Volkman BF, Bullerjahn GS, Biochemistry. 1999 Apr 20;38(16):4988-95. PMID:10213601
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