We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1npf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1npf.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1npf.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1npf| PDB=1npf | SCENE= }}
{{STRUCTURE_1npf| PDB=1npf | SCENE= }}
-
'''MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH NITRIC OXIDE'''
+
===MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH NITRIC OXIDE===
-
==Overview==
+
<!--
-
The interactions of nitric oxide (NO) and organic nitroso compounds with heme proteins are biologically important, and adduct formation between NO-containing compounds and myoglobin (Mb) have served as prototypical systems for studies of these interactions. We have prepared crystals of horse heart (hh) MbNO from nitrosylation of aqua-metMb crystals, and we have determined the crystal structure of hh MbNO at a resolution of 1.9 A. The Fe-N-O angle of 147 degrees in hh MbNO is larger than the corresponding 112 degrees angle previously determined from the crystal structure of sperm whale MbNO (Brucker et al., Proteins 1998;30:352-356) but is similar to the 150 degrees angle determined from a MS XAFS study of a frozen solution of hh MbNO (Rich et al., J Am Chem Soc 1998;120:10827-10836). The Fe-N(O) bond length of 2.0 A (this work) is longer than the 1.75 A distance determined from the XAFS study and suggests distal pocket influences on FeNO geometry. The nitrosyl N atom is located 3.0 A from the imidazole N(epsilon) atom of the distal His64 residue, suggesting electrostatic stabilization of the FeNO moiety by His64. The crystal structure of the nitrosoethane adduct of ferrous hh Mb was determined at a resolution of 1.7 A. The nitroso O atom of the EtNO ligand is located 2.7 A from the imidazole N(epsilon) atom of His64, suggesting a hydrogen bond interaction between these groups. To the best of our knowledge, the crystal structure of hh Mb(EtNO) is the first such determination of a nitrosoalkane adduct of a heme protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14517970}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14517970 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14517970}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: No]]
[[Category: No]]
[[Category: Oxygen storage]]
[[Category: Oxygen storage]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:49:04 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:13:45 2008''

Revision as of 04:13, 28 July 2008

Image:1npf.png

Template:STRUCTURE 1npf

MYOGLOBIN (HORSE HEART) WILD-TYPE COMPLEXED WITH NITRIC OXIDE

Template:ABSTRACT PUBMED 14517970

About this Structure

1NPF is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.

Reference

Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane., Copeland DM, West AH, Richter-Addo GB, Proteins. 2003 Nov 1;53(2):182-92. PMID:14517970

Page seeded by OCA on Mon Jul 28 07:13:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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