1eyr

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[[Image:1eyr.gif|left|200px]]
 
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{{Structure
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==Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP==
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|PDB= 1eyr |SIZE=350|CAPTION= <scene name='initialview01'>1eyr</scene>, resolution 2.20&Aring;
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<StructureSection load='1eyr' size='340' side='right'caption='[[1eyr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CDP:CYTIDINE-5&#39;-DIPHOSPHATE'>CDP</scene>
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<table><tr><td colspan='2'>[[1eyr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EYR FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/N-acylneuraminate_cytidylyltransferase N-acylneuraminate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.43 2.7.7.43]
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</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>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDP:CYTIDINE-5-DIPHOSPHATE'>CDP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eyr OCA], [https://pdbe.org/1eyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eyr RCSB], [https://www.ebi.ac.uk/pdbsum/1eyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eyr ProSAT]</span></td></tr>
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</table>
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'''Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP'''
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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==Overview==
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/1eyr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1eyr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The x-ray crystallographic structure of selenomethionyl cytosine-5'-monophosphate-acylneuraminate synthetase (CMP-NeuAc synthetase) from Neisseria meningitidis has been determined at 2.0-A resolution using multiple-wavelength anomalous dispersion phasing, and a second structure, in the presence of the substrate analogue CDP, has been determined at 2.2-A resolution by molecular replacement. This work identifies the active site residues for this class of enzyme for the first time. The detailed interactions between the enzyme and CDP within the mononucleotide-binding pocket are directly observed, and the acylneuraminate-binding pocket has also been identified. A model of acylneuraminate bound to CMP-NeuAc synthetase has been constructed and provides a structural basis for understanding the mechanism of production of "activated" sialic acids. Sialic acids are key saccharide components on the surface of mammalian cells and can be virulence factors in a variety of bacterial species (e.g. Neisseria, Haemophilus, group B streptococci, etc.). As such, the identification of the bacterial CMP-NeuAc synthetase active site can serve as a starting point for rational drug design strategies.
The x-ray crystallographic structure of selenomethionyl cytosine-5'-monophosphate-acylneuraminate synthetase (CMP-NeuAc synthetase) from Neisseria meningitidis has been determined at 2.0-A resolution using multiple-wavelength anomalous dispersion phasing, and a second structure, in the presence of the substrate analogue CDP, has been determined at 2.2-A resolution by molecular replacement. This work identifies the active site residues for this class of enzyme for the first time. The detailed interactions between the enzyme and CDP within the mononucleotide-binding pocket are directly observed, and the acylneuraminate-binding pocket has also been identified. A model of acylneuraminate bound to CMP-NeuAc synthetase has been constructed and provides a structural basis for understanding the mechanism of production of "activated" sialic acids. Sialic acids are key saccharide components on the surface of mammalian cells and can be virulence factors in a variety of bacterial species (e.g. Neisseria, Haemophilus, group B streptococci, etc.). As such, the identification of the bacterial CMP-NeuAc synthetase active site can serve as a starting point for rational drug design strategies.
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==About this Structure==
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Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP.,Mosimann SC, Gilbert M, Dombroswki D, To R, Wakarchuk W, Strynadka NC J Biol Chem. 2001 Mar 16;276(11):8190-6. Epub 2000 Dec 11. PMID:11113120<ref>PMID:11113120</ref>
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1EYR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EYR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structure of a sialic acid-activating synthetase, CMP-acylneuraminate synthetase in the presence and absence of CDP., Mosimann SC, Gilbert M, Dombroswki D, To R, Wakarchuk W, Strynadka NC, J Biol Chem. 2001 Mar 16;276(11):8190-6. Epub 2000 Dec 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11113120 11113120]
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</div>
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[[Category: N-acylneuraminate cytidylyltransferase]]
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<div class="pdbe-citations 1eyr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Neisseria meningitidis]]
[[Category: Neisseria meningitidis]]
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[[Category: Single protein]]
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[[Category: Dombrowski D]]
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[[Category: Dombrowski, D.]]
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[[Category: Gilbert M]]
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[[Category: Gilbert, M.]]
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[[Category: Mosimann SC]]
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[[Category: Mosimann, S C.]]
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[[Category: Strynadka NC]]
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[[Category: Strynadka, N C.]]
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[[Category: Wakarchuk W]]
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[[Category: Wakarchuk, W.]]
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[[Category: CDP]]
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[[Category: acylneuraminate]]
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[[Category: cdp]]
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[[Category: sialic acid]]
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[[Category: synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:43:03 2008''
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Current revision

Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP

PDB ID 1eyr

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