2bwi
From Proteopedia
(New page: 200px<br /> <applet load="2bwi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bwi, resolution 1.10Å" /> '''ATOMIC RESOLUTION S...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2BWI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ ]] with CU, ACT, NO2 and MLI as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BWI OCA]]. | + | 2BWI is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Achromobacter_cycloclastes Achromobacter cycloclastes]] with CU, ACT, NO2 and MLI as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BWI OCA]]. |
==Reference== | ==Reference== | ||
Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism., Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS, Proc Natl Acad Sci U S A. 2005 Aug 23;102(34):12041-6. Epub 2005 Aug 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16093314 16093314] | Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism., Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS, Proc Natl Acad Sci U S A. 2005 Aug 23;102(34):12041-6. Epub 2005 Aug 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16093314 16093314] | ||
| + | [[Category: Achromobacter cycloclastes]] | ||
| + | [[Category: Nitrite reductase (NO-forming)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Antonyuk, S.V.]] | [[Category: Antonyuk, S.V.]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:05:36 2007'' |
Revision as of 09:00, 30 October 2007
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ATOMIC RESOLUTION STRUCTURE OF NITRITE-SOAKED ACHROMOBACTER CYCLOCLASTES CU NITRITE REDUCTASE
Overview
Copper-containing nitrite reductases catalyze the reduction of nitrite to, nitric oxide (NO), a key step in denitrification that results in the loss, of terrestrial nitrogen to the atmosphere. They are found in a wide, variety of denitrifying bacteria and fungi of different physiology from a, range of soil and aquatic ecosystems. Structural analysis of potential, intermediates in the catalytic cycle is an important goal in understanding, enzyme mechanism. Using "crystal harvesting" and substrate-soaking, techniques, we have determined atomic resolution structures of four forms, of the green Cu-nitrite reductase, from the soil bacterium Achromobacter, cycloclastes. These structures are the resting state of the enzyme at 0.9, A, two species exhibiting different conformations of nitrite ... [(full description)]
About this Structure
2BWI is a [Single protein] structure of sequence from [Achromobacter cycloclastes] with CU, ACT, NO2 and MLI as [ligands]. Active as [Nitrite reductase (NO-forming)], with EC number [1.7.2.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism., Antonyuk SV, Strange RW, Sawers G, Eady RR, Hasnain SS, Proc Natl Acad Sci U S A. 2005 Aug 23;102(34):12041-6. Epub 2005 Aug 10. PMID:16093314
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