2bwi: Difference between revisions

Revision as of 17:42, 21 February 2008

ATOMIC RESOLUTION STRUCTURE OF NITRITE-SOAKED ACHROMOBACTER CYCLOCLASTES CU NITRITE REDUCTASE

OverviewOverview

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 bound at the catalytic type 2 Cu, one of which is stable and also has NO present, at 1.10 A and 1.15 A, and a stable form with the product NO bound side-on to the catalytic type 2 Cu, at 1.12 A resolution. These structures provide incisive insights into the initial binding of substrate, its repositioning before catalysis, bond breakage (O-NO), and the formation of a stable NO adduct.

About this StructureAbout this Structure

2BWI is a Single protein structure of sequence from Achromobacter cycloclastes with , , and as ligands. Active as Nitrite reductase (NO-forming), with EC number 1.7.2.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 16:42:24 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 ==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 bound at the, catalytic type 2 Cu, one of which is stable and also has NO present, at, 1.10 A and 1.15 A, and a stable form with the product NO bound side-on to, the catalytic type 2 Cu, at 1.12 A resolution. These structures provide, incisive insights into the initial binding of substrate, its repositioning, before catalysis, bond breakage (O-NO), and the formation of a stable NO, adduct.
+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 bound at the catalytic type 2 Cu, one of which is stable and also has NO present, at 1.10 A and 1.15 A, and a stable form with the product NO bound side-on to the catalytic type 2 Cu, at 1.12 A resolution. These structures provide incisive insights into the initial binding of substrate, its repositioning before catalysis, bond breakage (O-NO), and the formation of a stable NO adduct.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Nitrite reductase (NO-forming)]]
 [[Category: Single protein]]
-[[Category: Antonyuk, S.V.]]
+[[Category: Antonyuk, S V.]]
-[[Category: Eady, R.R.]]
+[[Category: Eady, R R.]]
-[[Category: Hasnain, S.S.]]
+[[Category: Hasnain, S S.]]
 [[Category: Sawers, G.]]
-[[Category: Strange, R.W.]]
+[[Category: Strange, R W.]]
 [[Category: ACT]]
 [[Category: CU]]
@@ Line 29: / Line 29: @@
 [[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:28:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:24 2008''