1np3
From Proteopedia
(New page: 200px<br /><applet load="1np3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1np3, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1np3.jpg|left|200px]]<br /><applet load="1np3" size=" | + | [[Image:1np3.jpg|left|200px]]<br /><applet load="1np3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1np3, resolution 2.00Å" /> | caption="1np3, resolution 2.00Å" /> | ||
'''Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa'''<br /> | '''Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Acetohydroxy acid isomeroreductase (AHIR) is a key enzyme in the | + | Acetohydroxy acid isomeroreductase (AHIR) is a key enzyme in the biosynthesis of branched-chain amino acids. We have determined the first crystal structure of a class I AHIR from Pseudomonas aeruginosa at 2.0 A resolution. Its dodecameric architecture of 23 point group symmetry is assembled of six dimeric units and dimerization is essential for the formation of the active site. The dimeric unit of P.aeruginosa AHIR partially superimposes with a three-domain monomer of spinach AHIR, a class II enzyme. This demonstrates that the so-called plant-specific insert in the middle of spinach AHIR is structurally and functionally equivalent to the C-terminal alpha-helical domain of P.aeruginosa AHIR, and the C-terminal alpha-helical domain was duplicated during evolution from the shorter, class I AHIRs to the longer, class II AHIRs. The dimeric unit of P.aeruginosa AHIR possesses a deep figure-of-eight knot, essentially identical with that in the spinach AHIR monomer. Thus, our work lowers the likelihood of the previous proposal that "domain duplication followed by exchange of a secondary structure element can be a source of such a knot in the protein structure" being correct. |
==About this Structure== | ==About this Structure== | ||
| - | 1NP3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Active as [http://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] Full crystallographic information is available from [http:// | + | 1NP3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Active as [http://en.wikipedia.org/wiki/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NP3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ahn, H | + | [[Category: Ahn, H J.]] |
[[Category: Cho, H.]] | [[Category: Cho, H.]] | ||
| - | [[Category: Eom, S | + | [[Category: Eom, S J.]] |
| - | [[Category: Lee, B | + | [[Category: Lee, B I.]] |
| - | [[Category: Suh, S | + | [[Category: Suh, S W.]] |
| - | [[Category: Yoon, H | + | [[Category: Yoon, H J.]] |
[[Category: a deep figure-of-eight knot]] | [[Category: a deep figure-of-eight knot]] | ||
[[Category: c-terminal alpha-helical domain]] | [[Category: c-terminal alpha-helical domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:30 2008'' |
Revision as of 12:08, 21 February 2008
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Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa
Overview
Acetohydroxy acid isomeroreductase (AHIR) is a key enzyme in the biosynthesis of branched-chain amino acids. We have determined the first crystal structure of a class I AHIR from Pseudomonas aeruginosa at 2.0 A resolution. Its dodecameric architecture of 23 point group symmetry is assembled of six dimeric units and dimerization is essential for the formation of the active site. The dimeric unit of P.aeruginosa AHIR partially superimposes with a three-domain monomer of spinach AHIR, a class II enzyme. This demonstrates that the so-called plant-specific insert in the middle of spinach AHIR is structurally and functionally equivalent to the C-terminal alpha-helical domain of P.aeruginosa AHIR, and the C-terminal alpha-helical domain was duplicated during evolution from the shorter, class I AHIRs to the longer, class II AHIRs. The dimeric unit of P.aeruginosa AHIR possesses a deep figure-of-eight knot, essentially identical with that in the spinach AHIR monomer. Thus, our work lowers the likelihood of the previous proposal that "domain duplication followed by exchange of a secondary structure element can be a source of such a knot in the protein structure" being correct.
About this Structure
1NP3 is a Single protein structure of sequence from Pseudomonas aeruginosa. Active as Ketol-acid reductoisomerase, with EC number 1.1.1.86 Full crystallographic information is available from OCA.
Reference
Crystal structure of class I acetohydroxy acid isomeroreductase from Pseudomonas aeruginosa., Ahn HJ, Eom SJ, Yoon HJ, Lee BI, Cho H, Suh SW, J Mol Biol. 2003 Apr 25;328(2):505-15. PMID:12691757
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