1gmv: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1gmv.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1gmv", 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_1gmv|  PDB=1gmv  |  SCENE=  }}
'''STRUCTURE OF UREE'''


==Structure of UreE==
<StructureSection load='1gmv' size='340' side='right'caption='[[1gmv]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gmv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GMV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=1gmv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmv OCA], [https://pdbe.org/1gmv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gmv RCSB], [https://www.ebi.ac.uk/pdbsum/1gmv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gmv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UREE_KLEAE UREE_KLEAE] Involved in urease metallocenter assembly. Binds about 6 nickel ions per homodimer. Probably functions as a nickel donor during metallocenter assembly. Its function can be bypassed in vitro in the presence of high nickel concentrations.[HAMAP-Rule:MF_00822]
== 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/gm/1gmv_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=1gmv ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
UreE is proposed to be a metallochaperone that delivers nickel ions to urease during activation of this bacterial virulence factor. Wild-type Klebsiella aerogenes UreE binds approximately six nickel ions per homodimer, whereas H144*UreE (a functional C-terminal truncated variant) was previously reported to bind two. We determined the structure of H144*UreE by multi-wavelength anomalous diffraction and refined it to 1.5 A resolution. The present structure reveals an Hsp40-like peptide-binding domain, an Atx1-like metal-binding domain, and a flexible C terminus. Three metal-binding sites per dimer, defined by structural analysis of Cu-H144*UreE, are on the opposite face of the Atx1-like domain than observed in the copper metallochaperone. One metal bridges the two subunits via the pair of His-96 residues, whereas the other two sites involve metal coordination by His-110 and His-112 within each subunit. In contrast to the copper metallochaperone mechanism involving thiol ligand exchanges between structurally similar chaperones and target proteins, we propose that the Hsp40-like module interacts with urease apoprotein and/or other urease accessory proteins, while the Atx1-like domain delivers histidyl-bound nickel to the urease active site.


==Overview==
Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation.,Song HK, Mulrooney SB, Huber R, Hausinger RP J Biol Chem. 2001 Dec 28;276(52):49359-64. Epub 2001 Oct 8. PMID:11591723<ref>PMID:11591723</ref>
UreE is proposed to be a metallochaperone that delivers nickel ions to urease during activation of this bacterial virulence factor. Wild-type Klebsiella aerogenes UreE binds approximately six nickel ions per homodimer, whereas H144*UreE (a functional C-terminal truncated variant) was previously reported to bind two. We determined the structure of H144*UreE by multi-wavelength anomalous diffraction and refined it to 1.5 A resolution. The present structure reveals an Hsp40-like peptide-binding domain, an Atx1-like metal-binding domain, and a flexible C terminus. Three metal-binding sites per dimer, defined by structural analysis of Cu-H144*UreE, are on the opposite face of the Atx1-like domain than observed in the copper metallochaperone. One metal bridges the two subunits via the pair of His-96 residues, whereas the other two sites involve metal coordination by His-110 and His-112 within each subunit. In contrast to the copper metallochaperone mechanism involving thiol ligand exchanges between structurally similar chaperones and target proteins, we propose that the Hsp40-like module interacts with urease apoprotein and/or other urease accessory proteins, while the Atx1-like domain delivers histidyl-bound nickel to the urease active site.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1GMV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMV OCA].
</div>
<div class="pdbe-citations 1gmv" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation., Song HK, Mulrooney SB, Huber R, Hausinger RP, J Biol Chem. 2001 Dec 28;276(52):49359-64. Epub 2001 Oct 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11591723 11591723]
*[[Urease accessory protein 3D structures|Urease accessory protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella aerogenes]]
[[Category: Klebsiella aerogenes]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hausinger, R.]]
[[Category: Hausinger R]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Mulrooney, S B.]]
[[Category: Mulrooney SB]]
[[Category: Song, H K.]]
[[Category: Song HK]]
[[Category: Metallochaperone]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:45:44 2008''

Latest revision as of 08:49, 9 May 2024

Structure of UreE

1gmv, resolution 2.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA