2tsa: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(9 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2tsa.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2tsa", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2tsa|  PDB=2tsa  |  SCENE=  }}
'''AZURIN MUTANT M121A'''


==AZURIN MUTANT M121A==
<StructureSection load='2tsa' size='340' side='right'caption='[[2tsa]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2tsa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tsa 1tsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TSA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2tsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2tsa OCA], [https://pdbe.org/2tsa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2tsa RCSB], [https://www.ebi.ac.uk/pdbsum/2tsa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2tsa ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE]] Transfers electrons from cytochrome c551 to cytochrome oxidase.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ts/2tsa_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2tsa ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of the azurin mutant Met121Ala and its azide derivative Met121Ala-azide from Pseudomonas aeruginosa have been determined. The final crystallographic R values are 21.3 and 19.4% for the two structures, respectively. In the Met121Ala mutant, the distance between the copper ion and His117 increases by 0.34 A compared with the wild-type structure. The removal of the methionine in the apical position induces a shortening of the distance from the copper ion to the carbonyl O atom of Gly45 from 2.97 to 2.74 A. In the Met121Ala-azide structure, the azide anion occupies the cavity created by replacing the Met121 side chain with the smaller methyl group of Ala. The azide anion binds with a terminal N atom to the copper ion at a distance of about 2.04 A. In addition, the copper ion has moved out of the trigonal plane by about 0.26 A towards the azide anion. Thus, the copper site in this structure has a distorted tetrahedral arrangement. The spectroscopic characteristics show, in addition, that the copper sites in the two structures are distinctively different. The Met121Ala mutant still maintains the properties of an ordinary type 1 copper site while the Met121Ala-azide derivative has an absorption maximum at about 409 nm and the copper hyperfine coupling has increased to a value intermediate between those of type 2 copper and the wild-type azurin.


==Overview==
Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative: crystal structures and spectral properties.,Tsai LC, Bonander N, Harata K, Karlsson G, Vanngard T, Langer V, Sjolin L Acta Crystallogr D Biol Crystallogr. 1996 Sep 1;52(Pt 5):950-8. PMID:15299604<ref>PMID:15299604</ref>
The crystal structures of the azurin mutant Met121Ala and its azide derivative Met121Ala-azide from Pseudomonas aeruginosa have been determined. The final crystallographic R values are 21.3 and 19.4% for the two structures, respectively. In the Met121Ala mutant, the distance between the copper ion and His117 increases by 0.34 A compared with the wild-type structure. The removal of the methionine in the apical position induces a shortening of the distance from the copper ion to the carbonyl O atom of Gly45 from 2.97 to 2.74 A. In the Met121Ala-azide structure, the azide anion occupies the cavity created by replacing the Met121 side chain with the smaller methyl group of Ala. The azide anion binds with a terminal N atom to the copper ion at a distance of about 2.04 A. In addition, the copper ion has moved out of the trigonal plane by about 0.26 A towards the azide anion. Thus, the copper site in this structure has a distorted tetrahedral arrangement. The spectroscopic characteristics show, in addition, that the copper sites in the two structures are distinctively different. The Met121Ala mutant still maintains the properties of an ordinary type 1 copper site while the Met121Ala-azide derivative has an absorption maximum at about 409 nm and the copper hyperfine coupling has increased to a value intermediate between those of type 2 copper and the wild-type azurin.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2TSA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tsa 1tsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TSA OCA].
</div>
<div class="pdbe-citations 2tsa" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative: crystal structures and spectral properties., Tsai LC, Bonander N, Harata K, Karlsson G, Vanngard T, Langer V, Sjolin L, Acta Crystallogr D Biol Crystallogr. 1996 Sep 1;52(Pt 5):950-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299604 15299604]
*[[Azurin 3D structures|Azurin 3D structures]]
[[Category: Pseudomonas aeruginosa]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Bonander, N.]]
__TOC__
[[Category: Harata, K.]]
</StructureSection>
[[Category: Karlsson, B G.]]
[[Category: Large Structures]]
[[Category: Langer, V.]]
[[Category: Bonander, N]]
[[Category: Sjolin, L.]]
[[Category: Harata, K]]
[[Category: Tsai, L C.]]
[[Category: Karlsson, B G]]
[[Category: Vanngard, T.]]
[[Category: Langer, V]]
[[Category: Sjolin, L]]
[[Category: Tsai, L C]]
[[Category: Vanngard, T]]
[[Category: Electron transport]]
[[Category: Electron transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:27:00 2008''

Latest revision as of 15:45, 3 November 2021

AZURIN MUTANT M121A

2tsa, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2tsa&oldid=3471733"