2gz2

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{{Seed}}
 
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[[Image:2gz2.png|left|200px]]
 
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==Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with 2',5'-ADP==
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The line below this paragraph, containing "STRUCTURE_2gz2", creates the "Structure Box" on the page.
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<StructureSection load='2gz2' size='340' side='right'caption='[[2gz2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2gz2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GZ2 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2P:ADENOSINE-2-5-DIPHOSPHATE'>A2P</scene></td></tr>
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{{STRUCTURE_2gz2| PDB=2gz2 | SCENE= }}
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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=2gz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gz2 OCA], [https://pdbe.org/2gz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gz2 RCSB], [https://www.ebi.ac.uk/pdbsum/2gz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gz2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0H2UPS5_STRPN A0A0H2UPS5_STRPN] Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.[HAMAP-Rule:MF_02121]
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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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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gz/2gz2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2gz2 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 ==
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Aspartate-beta-semialdehyde dehydrogenase (ASADH) catalyzes a critical branch point transformation in amino acid bio-synthesis. The products of the aspartate pathway are essential in microorganisms, and this entire pathway is absent in mammals, making this enzyme an attractive target for antibiotic development. The first structure of an ASADH from a Gram-positive bacterium, Streptococcus pneumoniae, has now been determined. The overall structure of the apoenzyme has a similar fold to those of the Gram-negative and archaeal ASADHs but contains some interesting structural variations that can be exploited for inhibitor design. Binding of the coenzyme NADP, as well as a truncated nucleotide analogue, into an alternative conformation from that observed in Gram-negative ASADHs causes an enzyme domain closure that precedes catalysis. The covalent acyl-enzyme intermediate was trapped by soaking the substrate into crystals of the coenzyme complex, and the structure of this elusive intermediate provides detailed insights into the catalytic mechanism.
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===Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with 2',5'-ADP===
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Examination of key intermediates in the catalytic cycle of aspartate-beta-semialdehyde dehydrogenase from a gram-positive infectious bacteria.,Faehnle CR, Le Coq J, Liu X, Viola RE J Biol Chem. 2006 Oct 13;281(41):31031-40. Epub 2006 Aug 8. PMID:16895909<ref>PMID:16895909</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2gz2" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16895909}}, adds the Publication Abstract to the page
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*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16895909 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16895909}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2GZ2 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZ2 OCA].
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==Reference==
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<ref group="xtra">PMID:16895909</ref><references group="xtra"/>
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[[Category: Aspartate-semialdehyde dehydrogenase]]
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[[Category: Streptococcus pneumoniae]]
[[Category: Streptococcus pneumoniae]]
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[[Category: Coq, J Le.]]
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[[Category: Faehnle CR]]
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[[Category: Faehnle, C R.]]
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[[Category: Le Coq J]]
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[[Category: Liu, X.]]
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[[Category: Liu X]]
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[[Category: Viola, R E.]]
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[[Category: Viola RE]]
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[[Category: Aspartate pathway]]
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[[Category: Dehydrogenase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:25:02 2009''
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Current revision

Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with 2',5'-ADP

PDB ID 2gz2

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