1aaj: Difference between revisions

Revision as of 16:29, 30 June 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:1aaj.png

Template:STRUCTURE 1aaj

CRYSTAL STRUCTURE ANALYSIS OF AMICYANIN AND APOAMICYANIN FROM PARACOCCUS DENITRIFICANS AT 2.0 ANGSTROMS AND 1.8 ANGSTROMS RESOLUTIONCRYSTAL STRUCTURE ANALYSIS OF AMICYANIN AND APOAMICYANIN FROM PARACOCCUS DENITRIFICANS AT 2.0 ANGSTROMS AND 1.8 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8495197

About this StructureAbout this Structure

1AAJ is a Single protein structure of sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure analysis of amicyanin and apoamicyanin from Paracoccus denitrificans at 2.0 A and 1.8 A resolution., Durley R, Chen L, Lim LW, Mathews FS, Davidson VL, Protein Sci. 1993 May;2(5):739-52. PMID:8495197

Page seeded by OCA on Mon Jun 30 16:29:30 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1aaj.gif|left|200px]]
+{{Seed}}
+[[Image:1aaj.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1aaj|  PDB=1aaj  |  SCENE=  }}
-'''CRYSTAL STRUCTURE ANALYSIS OF AMICYANIN AND APOAMICYANIN FROM PARACOCCUS DENITRIFICANS AT 2.0 ANGSTROMS AND 1.8 ANGSTROMS RESOLUTION'''
+===CRYSTAL STRUCTURE ANALYSIS OF AMICYANIN AND APOAMICYANIN FROM PARACOCCUS DENITRIFICANS AT 2.0 ANGSTROMS AND 1.8 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The crystal structure of amicyanin, a cupredoxin isolated from Paracoccus denitrificans, has been determined by molecular replacement. The structure has been refined at 2.0 A resolution using energy-restrained least-squares procedures to a crystallographic residual of 15.7%. The copper-free protein, apoamicyanin, has also been refined to 1.8 A resolution with residual 15.5%. The protein is found to have a beta-sandwich topology with nine beta-strands forming two mixed beta-sheets. The secondary structure is very similar to that observed in the other classes of cupredoxins, such as plastocyanin and azurin. Amicyanin has approximately 20 residues at the N-terminus that have no equivalents in the other proteins; a portion of these residues forms the first beta-strand of the structure. The copper atom is located in a pocket between the beta-sheets and is found to have four coordinating ligands: two histidine nitrogens, one cysteine sulfur, and, at a longer distance, one methionine sulfur. The geometry of the copper coordination is very similar to that in the plant plastocyanins. Three of the four copper ligands are located in the loop between beta-strands eight and nine. This loop is shorter than that in the other cupredoxins, having only two residues each between the cysteine and histidine and the histidine and methionine ligands. The amicyanin and apoamicyanin structures are very similar; in particular, there is little difference in the positions of the coordinating ligands with or without copper. One of the copper ligands, a histidine, lies close to the protein surface and is surrounded on that surface by seven hydrophobic residues. This hydrophobic patch is thought to be important as an electron transfer site.
+The line below this paragraph, {{ABSTRACT_PUBMED_8495197}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8495197 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8495197}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Mathews, F S.]]
 [[Category: Electron transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:02:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:29:30 2008''