2fem: Difference between revisions

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[[Image:2fem.gif|left|200px]]<br /><applet load="2fem" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2fem, resolution 1.90&Aring;" />
'''Mutant R188M of the Cytidine Monophosphate Kinase From E. Coli'''<br />


==About this Structure==
==Mutant R188M of the Cytidine Monophosphate Kinase From E. Coli==
2FEM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Cytidylate_kinase Cytidylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.14 2.7.4.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEM OCA].  
<StructureSection load='2fem' size='340' side='right'caption='[[2fem]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
[[Category: Cytidylate kinase]]
== Structural highlights ==
<table><tr><td colspan='2'>[[2fem]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FEM 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]] 1.9&#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=2fem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fem OCA], [https://pdbe.org/2fem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fem RCSB], [https://www.ebi.ac.uk/pdbsum/2fem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fem ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KCY_ECOLI KCY_ECOLI] ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.<ref>PMID:8190075</ref> <ref>PMID:7836281</ref>
== 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/fe/2fem_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=2fem ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Cytidine monophosphate kinase|Cytidine monophosphate kinase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Alexov, E.]]
[[Category: Alexov E]]
[[Category: Barzu, O.]]
[[Category: Barzu O]]
[[Category: Bertrand, T.]]
[[Category: Bertrand T]]
[[Category: Briozzo, P.]]
[[Category: Briozzo P]]
[[Category: Bucurenci, N.]]
[[Category: Bucurenci N]]
[[Category: Gilles, A M.]]
[[Category: Gilles AM]]
[[Category: Munier-Lehmann, H.]]
[[Category: Munier-Lehmann H]]
[[Category: Ofiteru, A.]]
[[Category: Ofiteru A]]
[[Category: Tourneux, L.]]
[[Category: Tourneux L]]
[[Category: nucleotide monophosphate kinase; transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:38 2008''

Latest revision as of 12:23, 14 February 2024

Mutant R188M of the Cytidine Monophosphate Kinase From E. ColiMutant R188M of the Cytidine Monophosphate Kinase From E. Coli

Structural highlights

2fem is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KCY_ECOLI ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Yamanaka K, Ogura T, Koonin EV, Niki H, Hiraga S. Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli. Mol Gen Genet. 1994 Apr;243(1):9-16. PMID:8190075
  2. ↑ Fricke J, Neuhard J, Kelln RA, Pedersen S. The cmk gene encoding cytidine monophosphate kinase is located in the rpsA operon and is required for normal replication rate in Escherichia coli. J Bacteriol. 1995 Feb;177(3):517-23. PMID:7836281

2fem, resolution 1.90Å

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