1uat

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1uat.jpg|left|200px]]<br /><applet load="1uat" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1uat.jpg|left|200px]]
-
caption="1uat, resolution 1.90&Aring;" />
+
 
-
'''The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J'''<br />
+
{{Structure
 +
|PDB= 1uat |SIZE=350|CAPTION= <scene name='initialview01'>1uat</scene>, resolution 1.90&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
 +
|ACTIVITY=
 +
|GENE=
 +
}}
 +
 
 +
'''The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1UAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methylomonas_sp._j Methylomonas sp. j] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAT OCA].
+
1UAT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methylomonas_sp._j Methylomonas sp. j]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UAT OCA].
==Reference==
==Reference==
-
The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J., Inoue T, Suzuki S, Nishio N, Yamaguchi K, Kataoka K, Tobari J, Yong X, Hamanaka S, Matsumura H, Kai Y, J Mol Biol. 2003 Oct 10;333(1):117-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14516747 14516747]
+
The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J., Inoue T, Suzuki S, Nishio N, Yamaguchi K, Kataoka K, Tobari J, Yong X, Hamanaka S, Matsumura H, Kai Y, J Mol Biol. 2003 Oct 10;333(1):117-24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14516747 14516747]
[[Category: Methylomonas sp. j]]
[[Category: Methylomonas sp. j]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 27: Line 36:
[[Category: beta-barrel]]
[[Category: beta-barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:33 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:29:35 2008''

Revision as of 12:29, 20 March 2008


PDB ID 1uat

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J


Overview

The obligate methylotroph Methylomonas sp. strain J produces two azurins (Az-iso1 and Az-iso2) as candidates for electron acceptor from methylamine dehydrogenase (MADH) in the electron-transfer process involving the oxidation of methylamine to formaldehyde and ammonia. The X-ray crystallographic study indicated that Az-iso2 gives two types of crystals (form I and form II) with polyethylene glycol (PEG4000) and ammonium sulfate as the precipitants, respectively. Comparison between the two Az-iso2 structures in forms I and II reveals the remarkable structural changes at the top surface of the molecule around the copper atom. Az-iso2 possesses Gly43 instead of Val43 or Ala43, which is unique among all other azurins around the copper ligand His46, inducing the remarkable structural change in the loop region from Gly37 to Gly43. When the structure of Az-iso2 is superimposed on that of amicyanin in the ternary complex composed of MADH, amicyanin, and cytochrome c(551), the loop of Az-iso2 deeply overlaps with the light subunit of MADH. However, the Az-iso2 molecule is probably able to avoid any steric hindrance with the cognate MADH to form the complex for intermolecular electron-transfer reaction, since the loop containing Gly43 is flexible. We discuss why the electron-transfer activity of Az-iso2 is fivefold higher than that of Az-iso1.

About this Structure

1UAT is a Single protein structure of sequence from Methylomonas sp. j. Full crystallographic information is available from OCA.

Reference

The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J., Inoue T, Suzuki S, Nishio N, Yamaguchi K, Kataoka K, Tobari J, Yong X, Hamanaka S, Matsumura H, Kai Y, J Mol Biol. 2003 Oct 10;333(1):117-24. PMID:14516747

Page seeded by OCA on Thu Mar 20 14:29:35 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools