1j02

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1j02.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1j02.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1j02| PDB=1j02 | SCENE= }}
{{STRUCTURE_1j02| PDB=1j02 | SCENE= }}
-
'''Crystal Structure of Rat Heme Oxygenase-1-Heme Bound to NO'''
+
===Crystal Structure of Rat Heme Oxygenase-1-Heme Bound to NO===
-
==Overview==
+
<!--
-
Heme oxygenase (HO) catalyzes heme degradation by utilizing O(2) and reducing equivalents to produce biliverdin IX alpha, iron, and CO. To avoid product inhibition, the heme[bond]HO complex (heme[bond]HO) is structured to markedly increase its affinity for O(2) while suppressing its affinity for CO. We determined the crystal structures of rat ferrous heme[bond]HO and heme[bond]HO bound to CO, CN(-), and NO at 2.3, 1.8, 2.0, and 1.7 A resolution, respectively. The heme pocket of ferrous heme-HO has the same conformation as that of the previously determined ferric form, but no ligand is visible on the distal side of the ferrous heme. Fe[bond]CO and Fe[bond]CN(-) are tilted, whereas the Fe[bond]NO is bent. The structure of heme[bond]HO bound to NO is identical to that bound to N(3)(-), which is also bent as in the case of O(2). Notably, in the CO- and CN(-)-bound forms, the heme and its ligands shift toward the alpha-meso carbon, and the distal F-helix shifts in the opposite direction. These shifts allow CO or CN(-) to bind in a tilted fashion without a collision between the distal ligand and Gly139 O and cause disruption of one salt bridge between the heme and basic residue. The structural identity of the ferrous and ferric states of heme[bond]HO indicates that these shifts are not produced on reduction of heme iron. Neither such conformational changes nor a heme shift occurs on NO or N(3)(-) binding. Heme[bond]HO therefore recognizes CO and O(2) by their binding geometries. The marked reduction in the ratio of affinities of CO to O(2) for heme[bond]HO achieved by an increase in O(2) affinity [Migita, C. T., Matera, K. M., Ikeda-Saito, M., Olson, J. S., Fujii, H., Yoshimura, T., Zhou, H., and Yoshida, T. (1998) J. Biol. Chem. 273, 945-949] is explained by hydrogen bonding and polar interactions that are favorable for O(2) binding, as well as by characteristic structural changes in the CO-bound form.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12924938}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12924938 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12924938}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Alpha helix]]
[[Category: Alpha helix]]
[[Category: O2-analog bound form]]
[[Category: O2-analog bound form]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:38:16 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:17:20 2008''

Revision as of 11:17, 1 July 2008

Image:1j02.png

Template:STRUCTURE 1j02

Crystal Structure of Rat Heme Oxygenase-1-Heme Bound to NO

Template:ABSTRACT PUBMED 12924938

About this Structure

1J02 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structures of ferrous and CO-, CN(-)-, and NO-bound forms of rat heme oxygenase-1 (HO-1) in complex with heme: structural implications for discrimination between CO and O2 in HO-1., Sugishima M, Sakamoto H, Noguchi M, Fukuyama K, Biochemistry. 2003 Aug 26;42(33):9898-905. PMID:12924938

Page seeded by OCA on Tue Jul 1 14:17:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1j02"
Personal tools