1b37

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(Difference between revisions)

Revision as of 23:19, 27 December 2023

A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE

Structural highlights

1b37 is a 3 chain structure with sequence from Zea mays. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAO1_MAIZE Flavoenzyme involved in polyamine back-conversion (Ref.4, PubMed:16331971). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (Ref.4, PubMed:16331971). Plays an important role in the regulation of polyamine intracellular concentration (Probable).^[1] ^[2] ^[3]

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

BACKGROUND: Polyamines are essential for cell growth and differentiation; compounds interfering with their metabolism are potential anticancer agents. Polyamine oxidase (PAO) plays a central role in polyamine homeostasis. The enzyme utilises an FAD cofactor to catalyse the oxidation of the secondary amino groups of spermine and spermidine. RESULTS: The first crystal structure of a polyamine oxidase has been determined to a resolution of 1.9 Angstroms. PAO from Zea mays contains two domains, which define a remarkable 30 Angstrom long U-shaped catalytic tunnel at their interface. The structure of PAO in complex with the inhibitor MDL72527 reveals the residues forming the catalytic machinery and unusual enzyme-inhibitor CH.O H bonds. A ring of glutamate and aspartate residues surrounding one of the two tunnel openings contributes to the steering of the substrate towards the inside of the tunnel. CONCLUSIONS: PAO specifically oxidizes substrates that have both primary and secondary amino groups. The complex with MDL72527 shows that the primary amino groups are essential for the proper alignment of the substrate with respect to the flavin. Conservation of an N-terminal sequence motif indicates that PAO is member of a novel family of flavoenzymes. Among these, monoamine oxidase displays significant sequence homology with PAO, suggesting a similar overall folding topology.

A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase.,Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A Structure. 1999 Mar 15;7(3):265-76. PMID:10368296^[4]

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

References

↑ Polticelli F, Basran J, Faso C, Cona A, Minervini G, Angelini R, Federico R, Scrutton NS, Tavladoraki P. Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase. Biochemistry. 2005 Dec 13;44(49):16108-20. PMID:16331971 doi:10.1021/bi050983i
↑ Polticelli F, Basran J, Faso C, Cona A, Minervini G, Angelini R, Federico R, Scrutton NS, Tavladoraki P. Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase. Biochemistry. 2005 Dec 13;44(49):16108-20. PMID:16331971 doi:10.1021/bi050983i
↑ Polticelli F, Basran J, Faso C, Cona A, Minervini G, Angelini R, Federico R, Scrutton NS, Tavladoraki P. Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase. Biochemistry. 2005 Dec 13;44(49):16108-20. PMID:16331971 doi:10.1021/bi050983i
↑ Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A. A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase. Structure. 1999 Mar 15;7(3):265-76. PMID:10368296

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b37"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1b37]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B37 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCA:ALPHA-D-FUCOSE'>FCA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17 1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FCA:ALPHA-D-FUCOSE'>FCA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1b37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b37 OCA], [https://pdbe.org/1b37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b37 RCSB], [https://www.ebi.ac.uk/pdbsum/1b37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b37 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PAO_MAIZE PAO_MAIZE]] Catalyzes the oxidation of the secondary amino group of polyamines (spermine, spermidine and their acetyl derivatives). Plays an important role in the regulation of polyamine intracellular concentration.
+[https://www.uniprot.org/uniprot/PAO1_MAIZE PAO1_MAIZE] Flavoenzyme involved in polyamine back-conversion (Ref.4, PubMed:16331971). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (Ref.4, PubMed:16331971). Plays an important role in the regulation of polyamine intracellular concentration (Probable).<ref>PMID:16331971</ref> <ref>PMID:16331971</ref> <ref>PMID:16331971</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Oxidoreductase]]
 [[Category: Zea mays]]
-[[Category: Angelini, R]]
+[[Category: Angelini R]]
-[[Category: Ascenzi, P]]
+[[Category: Ascenzi P]]
-[[Category: Binda, C]]
+[[Category: Binda C]]
-[[Category: Coda, A]]
+[[Category: Coda A]]
-[[Category: Federico, R]]
+[[Category: Federico R]]
-[[Category: Mattevi, A]]
+[[Category: Mattevi A]]
-[[Category: Flavin-dependent amine oxidase]]

1b37

From Proteopedia

Revision as of 23:19, 27 December 2023

A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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