4pty: Difference between revisions

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'''~~Unreleased~~ structure'''

==Crystal structure of the Escherichia coli alkanesulfonate FMN reductase SsuE in apo form==

== Structural highlights ==

<table><tr><td colspan='2'>[[4pty]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PTY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PTY FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ptz|4ptz]], [[4pu0|4pu0]]</td></tr>

<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FMN_reductase_(NADPH) FMN reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38 1.5.1.38] </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=4pty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pty OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pty RCSB], [http://www.ebi.ac.uk/pdbsum/4pty PDBsum]</span></td></tr>

<table>

== Publication Abstract from PubMed ==

The Escherichia coli sulfur starvation utilization (ssu) operon includes a two-component monooxygenase system consisting of a nicotinamide adenine dinucleotide phosphate (NADPH)-dependent flavin mononucleotide (FMN) reductase, SsuE, and a monooxygenase, SsuD. SsuE is part of the flavodoxin-like superfamily, and we report here the crystal structures of its apo, FMN-bound, and FMNH2-bound forms at approximately 2 A resolution. In the crystals, SsuE forms a tetramer that is a dimer of dimers similar to those seen for homologous FMN reductases, quinone reductases, and the WrbA family of enzymes. A pi-helix present at the tetramer building interface is unique to the reductases from two-component monooxygenase systems. Analytical ultracentrifugation studies of SsuE confirm a dimer-tetramer equilibrium exists in solution, with FMN binding favoring the dimer. As the active site includes residues from both subunits, at least a dimeric association is required for the function of SsuE. The structures show that one FMN binds tightly in a deeply held site, which makes available a second binding site, in which either a second FMN or the nicotinamide of NADPH can bind. The FMNH2-bound structure shows subtle changes consistent with its binding being weaker than that of FMN. Combining this information with published kinetic studies, we propose a general catalytic cycle for two-component reductases of the flavodoxin-like superfamily, by which the enzyme can potentially provide FMNH2 to its partner monooxygenase by different routes depending on the FMN concentration and the presence of a partner monooxygenase.

~~The entry 4pty is ON HOLD until Paper Publication~~

Crystal Structure of Escherichia coli SsuE: Defining a General Catalytic Cycle for FMN Reductases of the Flavodoxin-like Superfamily.,Driggers CM, Dayal PV, Ellis HR, Karplus PA Biochemistry. 2014 Jun 3;53(21):3509-19. doi: 10.1021/bi500314f. Epub 2014 May, 21. PMID:24816272<ref>PMID:24816272</ref>

~~Authors~~: Driggers, C.M., Ellis, H.R., Karplus, P.A.

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

</div>

~~Description~~: ~~Crystal structure of the Escherichia coli alkanesulfonate FMN~~ reductase ~~SsuE in apo form~~

== References ==

__TOC__

</StructureSection>

[[Category: Driggers, C M.]]

[[Category: Ellis, H R.]]

[[Category: Karplus, P A.]]

[[Category: Flavodoxin-like fold]]

[[Category: Nadph-dependent fmn reductase]]

[[Category: Oxidoreductase]]

[[Category: Ssud]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of the Escherichia coli alkanesulfonate FMN reductase SsuE in apo form==
+<StructureSection load='4pty' size='340' side='right' caption='[[4pty]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4pty]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PTY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PTY FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ptz|4ptz]], [[4pu0|4pu0]]</td></tr>
+<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/FMN_reductase_(NADPH) FMN reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.38 1.5.1.38] </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=4pty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pty OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pty RCSB], [http://www.ebi.ac.uk/pdbsum/4pty PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The Escherichia coli sulfur starvation utilization (ssu) operon includes a two-component monooxygenase system consisting of a nicotinamide adenine dinucleotide phosphate (NADPH)-dependent flavin mononucleotide (FMN) reductase, SsuE, and a monooxygenase, SsuD. SsuE is part of the flavodoxin-like superfamily, and we report here the crystal structures of its apo, FMN-bound, and FMNH2-bound forms at approximately 2 A resolution. In the crystals, SsuE forms a tetramer that is a dimer of dimers similar to those seen for homologous FMN reductases, quinone reductases, and the WrbA family of enzymes. A pi-helix present at the tetramer building interface is unique to the reductases from two-component monooxygenase systems. Analytical ultracentrifugation studies of SsuE confirm a dimer-tetramer equilibrium exists in solution, with FMN binding favoring the dimer. As the active site includes residues from both subunits, at least a dimeric association is required for the function of SsuE. The structures show that one FMN binds tightly in a deeply held site, which makes available a second binding site, in which either a second FMN or the nicotinamide of NADPH can bind. The FMNH2-bound structure shows subtle changes consistent with its binding being weaker than that of FMN. Combining this information with published kinetic studies, we propose a general catalytic cycle for two-component reductases of the flavodoxin-like superfamily, by which the enzyme can potentially provide FMNH2 to its partner monooxygenase by different routes depending on the FMN concentration and the presence of a partner monooxygenase.
-The entry 4pty is ON HOLD  until Paper Publication
+Crystal Structure of Escherichia coli SsuE: Defining a General Catalytic Cycle for FMN Reductases of the Flavodoxin-like Superfamily.,Driggers CM, Dayal PV, Ellis HR, Karplus PA Biochemistry. 2014 Jun 3;53(21):3509-19. doi: 10.1021/bi500314f. Epub 2014 May, 21. PMID:24816272<ref>PMID:24816272</ref>
-Authors: Driggers, C.M., Ellis, H.R., Karplus, P.A.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of the Escherichia coli alkanesulfonate FMN reductase SsuE in apo form
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Driggers, C M.]]
+[[Category: Ellis, H R.]]
+[[Category: Karplus, P A.]]
+[[Category: Flavodoxin-like fold]]
+[[Category: Nadph-dependent fmn reductase]]
+[[Category: Oxidoreductase]]
+[[Category: Ssud]]