1rky

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1rky.gif|left|200px]]
[[Image:1rky.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1rky |SIZE=350|CAPTION= <scene name='initialview01'>1rky</scene>, resolution 1.68&Aring;
+
The line below this paragraph, containing "STRUCTURE_1rky", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</scene>, <scene name='pdbligand=XE:XENON'>XE</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-lysine_6-oxidase Protein-lysine 6-oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.13 1.4.3.13] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE= ATCC 28, 485 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4922 Pichia pastoris])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1rky| PDB=1rky | SCENE= }}
-
|RELATEDENTRY=[[1n9e|1N9E]], [[1rjo|1RJO]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rky OCA], [http://www.ebi.ac.uk/pdbsum/1rky PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rky RCSB]</span>
+
-
}}
+
'''PPLO + Xe'''
'''PPLO + Xe'''
Line 28: Line 25:
[[Category: Duff, A P.]]
[[Category: Duff, A P.]]
[[Category: Guss, J M.]]
[[Category: Guss, J M.]]
-
[[Category: amine oxidase]]
+
[[Category: Amine oxidase]]
-
[[Category: cao]]
+
[[Category: Cao]]
-
[[Category: copper-containing]]
+
[[Category: Copper-containing]]
-
[[Category: cuao]]
+
[[Category: Cuao]]
-
[[Category: dioxygen binding site]]
+
[[Category: Dioxygen binding site]]
-
[[Category: lysyl oxidase]]
+
[[Category: Lysyl oxidase]]
-
[[Category: oxygen binding site]]
+
[[Category: Oxygen binding site]]
-
[[Category: pplo]]
+
[[Category: Pplo]]
-
[[Category: quinone]]
+
[[Category: Quinone]]
-
[[Category: tpq]]
+
[[Category: Tpq]]
-
[[Category: trihydroxyphenylalanine quinone]]
+
[[Category: Trihydroxyphenylalanine quinone]]
-
[[Category: xenon]]
+
[[Category: Xenon]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:37:31 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:29:38 2008''
+

Revision as of 04:37, 3 May 2008

Image:1rky.gif

Template:STRUCTURE 1rky

PPLO + Xe


Overview

Potential dioxygen-binding sites in three Cu amine oxidases have been investigated by recording X-ray diffraction data at 1.7-2.2A resolution for crystals under a high pressure of xenon gas. Electron-density difference maps and crystallographic refinement provide unequivocal evidence for a number of Xe-binding sites in each enzyme. Only one of these sites is present in all three Cu amine oxidases studied. Structural changes elsewhere in the protein molecules are insignificant. The results illustrate the use of xenon as a probe for cavities, in which a protein may accommodate a dioxygen molecule. The finding of a potential dioxygen-binding cavity close to the active site of Cu amine oxidases may be relevant to the function of the enzymes, since the formation of a transient protein-dioxygen complex is a likely step in the catalytic mechanism. No evidence was found for xenon binding in a region of the molecule that was previously identified in two other Cu amine oxidases as a potential transient dioxygen-binding site.

About this Structure

1RKY is a Single protein structure of sequence from Pichia pastoris. Full crystallographic information is available from OCA.

Reference

Using xenon as a probe for dioxygen-binding sites in copper amine oxidases., Duff AP, Trambaiolo DM, Cohen AE, Ellis PJ, Juda GA, Shepard EM, Langley DB, Dooley DM, Freeman HC, Guss JM, J Mol Biol. 2004 Nov 26;344(3):599-607. PMID:15533431 Page seeded by OCA on Sat May 3 07:37:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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