1i74: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
m Protected "1i74" [edit=sysop:move=sysop]
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1i74.png|left|200px]]


{{STRUCTURE_1i74| PDB=1i74 | SCENE= }}
==STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE==
<StructureSection load='1i74' size='340' side='right'caption='[[1i74]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1i74]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I74 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1i74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i74 OCA], [https://pdbe.org/1i74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i74 RCSB], [https://www.ebi.ac.uk/pdbsum/1i74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i74 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPAC_STRMU PPAC_STRMU]
== 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/i7/1i74_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1i74 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Streptococcus mutans pyrophosphatase (Sm-PPase) is a member of a relatively uncommon but widely dispersed sequence family (family II) of inorganic pyrophosphatases. A structure will answer two main questions: is it structurally similar to the family I PPases, and is the mechanism similar? RESULTS: The first family II PPase structure, that of homodimeric Sm-PPase complexed with metal and sulfate ions, has been solved by X-ray crystallography at 2.2 A resolution. The tertiary fold of Sm-PPase consists of a 189 residue alpha/beta N-terminal domain and a 114 residue mixed beta sheet C-terminal domain and bears no resemblance to family I PPase, even though the arrangement of active site ligands and the residues that bind them shows significant similarity. The preference for Mn2+ over Mg2+ in family II PPases is explained by the histidine ligands and bidentate carboxylate coordination. The active site is located at the domain interface. The C-terminal domain is hinged to the N-terminal domain and exists in both closed and open conformations. CONCLUSIONS: The active site similiarities, including a water coordinated to two metal ions, suggest that the family II PPase mechanism is "analogous" (not "homologous") to that of family I PPases. This is a remarkable example of convergent evolution. The large change in C-terminal conformation suggests that domain closure might be the mechanism by which Sm-PPase achieves specificity for pyrophosphate over other polyphosphates.


===STREPTOCOCCUS MUTANS INORGANIC PYROPHOSPHATASE===
Crystal structure of Streptococcus mutans pyrophosphatase: a new fold for an old mechanism.,Merckel MC, Fabrichniy IP, Salminen A, Kalkkinen N, Baykov AA, Lahti R, Goldman A Structure. 2001 Apr 4;9(4):289-97. PMID:11525166<ref>PMID:11525166</ref>


{{ABSTRACT_PUBMED_11525166}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1i74" style="background-color:#fffaf0;"></div>
[[1i74]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I74 OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:011525166</ref><references group="xtra"/>
</StructureSection>
[[Category: Inorganic diphosphatase]]
[[Category: Large Structures]]
[[Category: Streptococcus mutans]]
[[Category: Streptococcus mutans]]
[[Category: Fabrichniy, I P.]]
[[Category: Fabrichniy IP]]
[[Category: Goldman, A.]]
[[Category: Goldman A]]
[[Category: Lahti, R.]]
[[Category: Lahti R]]
[[Category: Merckel, M C.]]
[[Category: Merckel MC]]
[[Category: Salminen, A.]]
[[Category: Salminen A]]
[[Category: Hydrolase]]
Retrieved from "https://proteopedia.org/1i74"