2bwd
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:2bwd.gif|left|200px]]<br /> | + | [[Image:2bwd.gif|left|200px]]<br /><applet load="2bwd" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2bwd" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2bwd, resolution 1.15Å" /> | caption="2bwd, resolution 1.15Å" /> | ||
'''ATOMIC RESOLUTION STRUCTURE OF ACHROMOBACTER CYCLOCLASTES CU NITRITE REDUCTASE WITH ENDOGENOUSLY BOUND NITRITE AND NO'''<br /> | '''ATOMIC RESOLUTION STRUCTURE OF ACHROMOBACTER CYCLOCLASTES CU NITRITE REDUCTASE WITH ENDOGENOUSLY BOUND NITRITE AND NO'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2BWD 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, MLI and NO 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] | + | 2BWD 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, MLI and NO 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] Known structural/functional Site: <scene name='pdbsite=AC1:Act Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BWD OCA]. |
==Reference== | ==Reference== | ||
| Line 31: | Line 30: | ||
[[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 Dec 18 19:00:43 2007'' |
Revision as of 16:50, 18 December 2007
|
ATOMIC RESOLUTION STRUCTURE OF ACHROMOBACTER CYCLOCLASTES CU NITRITE REDUCTASE WITH ENDOGENOUSLY BOUND NITRITE AND NO
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.
About this Structure
2BWD is a Single protein structure of sequence from Achromobacter cycloclastes with CU, ACT, NO2, MLI and NO 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.
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
Page seeded by OCA on Tue Dec 18 19:00:43 2007
