1jdo: Difference between revisions

Revision as of 20:05, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jdo.png

Template:STRUCTURE 1jdo

SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)

Template:ABSTRACT PUBMED 9533619

About this StructureAbout this Structure

1JDO is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

ReferenceReference

Nitric oxide myoglobin: crystal structure and analysis of ligand geometry., Brucker EA, Olson JS, Ikeda-Saito M, Phillips GN Jr, Proteins. 1998 Mar 1;30(4):352-6. PMID:9533619

Page seeded by OCA on Tue Jul 1 20:05:06 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1jdo.gif|left|200px]]
+{{Seed}}
+[[Image:1jdo.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1jdo|  PDB=1jdo  |  SCENE=  }}
-'''SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)'''
+===SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)===
-==Overview==
+<!--
-The structure of the ferrous nitric oxide form of native sperm whale myoglobin has been determined by X-ray crystallography to 1.7 angstroms resolution. The nitric oxide ligand is bent with respect to the heme plane: the Fe-N-O angle is 112 degrees. This angle is smaller than those observed in model compounds and in lupin leghemoglobin. The exact angle appears to be influenced by the strength of the proximal bond and hydrogen bonding interactions between the distal histidine and the bound ligand. Specifically, the N(epsilon) atom of histidine64 is located 2.8 angstroms away from the nitrogen atom of the bound ligand, implying electrostatic stabilization of the FeNO complex. This interpretation is supported by mutagenesis studies. When histidine64 is replaced with apolar amino acids, the rate of nitric oxide dissociation from myoglobin increases tenfold.
+The line below this paragraph, {{ABSTRACT_PUBMED_9533619}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9533619 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9533619}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Oxygen storage]]
 [[Category: Oxygen transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:05:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 20:05:06 2008''