We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2gz3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:14, 17 October 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2gz3.gif|left|200px]]<br /><applet load="2gz3" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2gz3, resolution 2.100&Aring;" />
 
-
'''Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with NADP and aspartate-semialdehyde'''<br />
 
-
==Overview==
+
==Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with NADP and aspartate-semialdehyde==
-
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.
+
<StructureSection load='2gz3' size='340' side='right'caption='[[2gz3]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2gz3]] is a 4 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=2GZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GZ3 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]] 2.1&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AS2:(2R)-2-AMINO-4-OXOBUTANOIC+ACID'>AS2</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=2gz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gz3 OCA], [https://pdbe.org/2gz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gz3 RCSB], [https://www.ebi.ac.uk/pdbsum/2gz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gz3 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[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]
 +
== 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/gz/2gz3_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=2gz3 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
==About this Structure==
+
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>
-
2GZ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae] with <scene name='pdbligand=NAP:'>NAP</scene> and <scene name='pdbligand=AS2:'>AS2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] Known structural/functional Sites: <scene name='pdbsite=AC1:Nap+Binding+Site+For+Residue+A+367'>AC1</scene>, <scene name='pdbsite=AC2:Nap+Binding+Site+For+Residue+B+367'>AC2</scene>, <scene name='pdbsite=AC3:Nap+Binding+Site+For+Residue+C+367'>AC3</scene>, <scene name='pdbsite=AC4:Nap+Binding+Site+For+Residue+D+367'>AC4</scene>, <scene name='pdbsite=AC5:As2+Binding+Site+For+Residue+A+400'>AC5</scene>, <scene name='pdbsite=AC6:As2+Binding+Site+For+Residue+B+400'>AC6</scene>, <scene name='pdbsite=AC7:As2+Binding+Site+For+Residue+C+400'>AC7</scene> and <scene name='pdbsite=AC8:As2+Binding+Site+For+Residue+D+400'>AC8</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GZ3 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16895909 16895909]
+
</div>
-
[[Category: Aspartate-semialdehyde dehydrogenase]]
+
<div class="pdbe-citations 2gz3" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Streptococcus pneumoniae]]
+
-
[[Category: Coq, J.Le.]]
+
-
[[Category: Faehnle, C.R.]]
+
-
[[Category: Liu, X.]]
+
-
[[Category: Viola, R.E.]]
+
-
[[Category: AS2]]
+
-
[[Category: NAP]]
+
-
[[Category: aspartate pathway]]
+
-
[[Category: dehydrogenase]]
+
-
[[Category: oxidoreductase]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:17:20 2008''
+
==See Also==
 +
*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Streptococcus pneumoniae]]
 +
[[Category: Faehnle CR]]
 +
[[Category: Le Coq J]]
 +
[[Category: Liu X]]
 +
[[Category: Viola RE]]

Current revision

Structure of Aspartate Semialdehyde Dehydrogenase (ASADH) from Streptococcus pneumoniae complexed with NADP and aspartate-semialdehyde

PDB ID 2gz3

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2gz3"
Personal tools