1bvb: Difference between revisions

Line 1:

[[Image:1bvb.~~gif~~|left|200px]]

[[Image:1bvb.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~HEME-PACKING MOTIFS REVEALED BY THE CRYSTAL STRUCTURE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA~~'''~~

===HEME-PACKING MOTIFS REVEALED BY THE CRYSTAL STRUCTURE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA===

~~==Overview==~~

<!--

~~Cytochrome c554 (cyt c554)~~, ~~a tetra-heme cytochrome from Nitrosomonas europaea~~, ~~is an essential component in~~ the ~~biological nitrification pathway. In N. europaea, ammonia is converted~~ to ~~hydroxylamine, which is then oxidized to nitrite by hydroxylamine oxidoreductase~~ (~~HAO). Cyt c554 functions in the latter process by accepting pairs of electrons from HAO and transferring them to a cytochrome acceptor. The crystal structure of cyt c554~~ at 2.~~6 A resolution shows a predominantly alpha-helical protein with four covalently attached hemes~~. ~~The four hemes are arranged in two pairs such that the planes of~~ the ~~porphyrin rings are almost parallel and overlapping at the edge; corresponding heme arrangements are observed in other multi-heme proteins~~. ~~Striking structural similarities are evident between the tetra~~-~~heme core of cyt c554 and hemes 3~~-~~6 of HAO, which suggests an evolutionary relationship between these redox partners.~~

The line below this paragraph, {{ABSTRACT_PUBMED_9808046}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9808046 is the PubMed ID number.

-->

==About this Structure==

Line 31:

Line 35:

[[Category: Cytochrome]]

[[Category: Electron transport]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:59:45 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:46:26 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1bvb.gif|left|200px]]
+{{Seed}}
+[[Image:1bvb.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1bvb|  PDB=1bvb  |  SCENE=  }}
-'''HEME-PACKING MOTIFS REVEALED BY THE CRYSTAL STRUCTURE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''
+===HEME-PACKING MOTIFS REVEALED BY THE CRYSTAL STRUCTURE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA===
-==Overview==
+<!--
-Cytochrome c554 (cyt c554), a tetra-heme cytochrome from Nitrosomonas europaea, is an essential component in the biological nitrification pathway. In N. europaea, ammonia is converted to hydroxylamine, which is then oxidized to nitrite by hydroxylamine oxidoreductase (HAO). Cyt c554 functions in the latter process by accepting pairs of electrons from HAO and transferring them to a cytochrome acceptor. The crystal structure of cyt c554 at 2.6 A resolution shows a predominantly alpha-helical protein with four covalently attached hemes. The four hemes are arranged in two pairs such that the planes of the porphyrin rings are almost parallel and overlapping at the edge; corresponding heme arrangements are observed in other multi-heme proteins. Striking structural similarities are evident between the tetra-heme core of cyt c554 and hemes 3-6 of HAO, which suggests an evolutionary relationship between these redox partners.
+The line below this paragraph, {{ABSTRACT_PUBMED_9808046}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9808046 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9808046}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Cytochrome]]
 [[Category: Electron transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:59:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:46:26 2008''