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2wet

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Revision as of 06:30, 10 October 2014

CRYSTAL STRUCTURE OF TRYPTOPHAN 5-HALOGENASE (PYRH) COMPLEX WITH FAD (TRYPTOPHAN)

Structural highlights

2wet is a 4 chain structure with sequence from Streptomyces rugosporus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	2wes, 2weu
Resources:	FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

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

Publication Abstract from PubMed

The regioselectively controlled introduction of chlorine into organic molecules is an important biological and chemical process. This importance derives from the observation that many pharmaceutically active natural products contain a chlorine atom. Flavin-dependent halogenases are one of the principal enzyme families responsible for regioselective halogenation of natural products. Structural studies of two flavin-dependent tryptophan 7-halogenases (PrnA and RebH) have generated important insights into the chemical mechanism of halogenation by this enzyme family. These proteins comprise two modules: a flavin adenine dinucleotide (FAD)-binding module and a tryptophan-binding module. Although the 7-halogenase studies advance a hypothesis for regioselectivity, this has never been experimentally demonstrated. PyrH is a tryptophan 5-halogenase that catalyzes halogenation on tryptophan C5 position. We report the crystal structure of a tryptophan 5-halogenase (PyrH) bound to tryptophan and FAD. The FAD-binding module is essentially unchanged relative to PrnA (and RebH), and PyrH would appear to generate the same reactive species from Cl(-), O(2), and 1,5-dihydroflavin adenine dinucleotide. We report additional mutagenesis data that extend our mechanistic understanding of this process, in particular highlighting a strap region that regulates FAD binding, and may allow communication between the two modules. PyrH has a significantly different tryptophan-binding module. The data show that PyrH binds tryptophan and presents the C5 atom to the reactive chlorinating species, shielding other potential reactive sites. We have mutated residues identified by structural analysis as recognizing the tryptophan in order to confirm their role. This work establishes the method by which flavin-dependent tryptophan halogenases regioselectively control chlorine addition to tryptophan. This method would seem to be general across the superfamily.

Structural insights into regioselectivity in the enzymatic chlorination of tryptophan.,Zhu X, De Laurentis W, Leang K, Herrmann J, Ihlefeld K, van Pee KH, Naismith JH J Mol Biol. 2009 Aug 7;391(1):74-85. Epub 2009 Jun 6. PMID:19501593^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhu X, De Laurentis W, Leang K, Herrmann J, Ihlefeld K, van Pee KH, Naismith JH. Structural insights into regioselectivity in the enzymatic chlorination of tryptophan. J Mol Biol. 2009 Aug 7;391(1):74-85. Epub 2009 Jun 6. PMID:19501593 doi:10.1016/j.jmb.2009.06.008

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2wet"

@@ Line 2: / Line 2: @@
 <StructureSection load='2wet' size='340' side='right' caption='[[2wet]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2wet]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_rugosporus Streptomyces rugosporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WET OCA]. <br>
+<table><tr><td colspan='2'>[[2wet]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_rugosporus Streptomyces rugosporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WET FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wes|2wes]], [[2weu|2weu]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wes|2wes]], [[2weu|2weu]]</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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wet OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wet RCSB], [http://www.ebi.ac.uk/pdbsum/2wet PDBsum]</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=2wet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wet OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wet RCSB], [http://www.ebi.ac.uk/pdbsum/2wet PDBsum]</span></td></tr>
+</table>
-<table>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 24: / Line 23: @@
 Structural insights into regioselectivity in the enzymatic chlorination of tryptophan.,Zhu X, De Laurentis W, Leang K, Herrmann J, Ihlefeld K, van Pee KH, Naismith JH J Mol Biol. 2009 Aug 7;391(1):74-85. Epub 2009 Jun 6. PMID:19501593<ref>PMID:19501593</ref>
-From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
 == References ==

2wet

From Proteopedia

Revision as of 06:30, 10 October 2014

CRYSTAL STRUCTURE OF TRYPTOPHAN 5-HALOGENASE (PYRH) COMPLEX WITH FAD (TRYPTOPHAN)

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

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