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[[Image:2ybo.png|left|200px]]
==THE X-RAY STRUCTURE OF THE SAM-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE NIRE FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH SAH==
<StructureSection load='2ybo' size='340' side='right' caption='[[2ybo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ybo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YBO OCA]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ybq|2ybq]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ybo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ybo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ybo RCSB], [http://www.ebi.ac.uk/pdbsum/2ybo PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
During the biosynthesis of heme d(1), the essential cofactor of cytochrome cd(1) nitrite reductase, the NirE protein catalyzes the methylation of uroporphyrinogen III to precorrin-2 using S-adenosyl-L-methionine (SAM) as the methyl group donor. The crystal structure of Pseudomonas aeruginosa NirE in complex with its substrate uroporphyrinogen III and the reaction by-product S-adenosyl-L-homocysteine (SAH) was solved to 2.0 A resolution. This represents the first enzyme-substrate complex structure for a SAM-dependent uroporphyrinogen III methyltransferase. The large substrate binds on top of the SAH in a "puckered" conformation in which the two pyrrole rings facing each other point into the same direction either upward or downward. Three arginine residues, a histidine, and a methionine are involved in the coordination of uroporphyrinogen III. Through site-directed mutagenesis of the nirE gene and biochemical characterization of the corresponding NirE variants the amino acid residues Arg-111, Glu-114, and Arg-149 were identified to be involved in NirE catalysis. Based on our structural and biochemical findings, we propose a potential catalytic mechanism for NirE in which the methyl transfer reaction is initiated by an arginine catalyzed proton abstraction from the C-20 position of the substrate.


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Crystal structure of the heme d1 biosynthesis enzyme NirE in complex with its substrate reveals new insights into the catalytic mechanism of S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferases.,Storbeck S, Saha S, Krausze J, Klink BU, Heinz DW, Layer G J Biol Chem. 2011 Jul 29;286(30):26754-67. Epub 2011 May 31. PMID:21632530<ref>PMID:21632530</ref>
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===THE X-RAY STRUCTURE OF THE SAM-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE NIRE FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH SAH===
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
== References ==
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{{ABSTRACT_PUBMED_21632530}}
 
==About this Structure==
[[2ybo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YBO OCA].
 
==Reference==
<ref group="xtra">PMID:021632530</ref><references group="xtra"/>
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Uroporphyrinogen-III C-methyltransferase]]
[[Category: Uroporphyrinogen-III C-methyltransferase]]
Retrieved from "https://proteopedia.org/2ybo"