1b37

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1b37" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b37, resolution 1.9&Aring;" /> '''A 30 ANGSTROM U-SHAPE...)
Current revision (08:20, 6 November 2024) (edit) (undo)
 
(19 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1b37.gif|left|200px]]<br /><applet load="1b37" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1b37, resolution 1.9&Aring;" />
 
-
'''A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE'''<br />
 
-
==Overview==
+
==A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE==
-
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.
+
<StructureSection load='1b37' size='340' side='right'caption='[[1b37]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 +
== 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='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='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/PAO1_MAIZE PAO1_MAIZE] Flavoenzyme involved in polyamine back-conversion (PubMed:16331971, Ref.4). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (PubMed:16331971, Ref.4). 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]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b3/1b37_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=1b37 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
==About this Structure==
+
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<ref>PMID:10368296</ref>
-
1B37 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with NAG and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Polyamine_oxidase Polyamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.11 1.5.3.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B37 OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368296 10368296]
+
</div>
-
[[Category: Polyamine oxidase]]
+
<div class="pdbe-citations 1b37" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Zea mays]]
+
-
[[Category: Angelini, R.]]
+
-
[[Category: Ascenzi, P.]]
+
-
[[Category: Binda, C.]]
+
-
[[Category: Coda, A.]]
+
-
[[Category: Federico, R.]]
+
-
[[Category: Mattevi, A.]]
+
-
[[Category: FAD]]
+
-
[[Category: NAG]]
+
-
[[Category: flavin-dependent amine oxidase]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:19:12 2007''
+
==See Also==
 +
*[[Polyamine oxidase|Polyamine oxidase]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Zea mays]]
 +
[[Category: Angelini R]]
 +
[[Category: Ascenzi P]]
 +
[[Category: Binda C]]
 +
[[Category: Coda A]]
 +
[[Category: Federico R]]
 +
[[Category: Mattevi A]]

Current revision

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

PDB ID 1b37

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/1b37"
Personal tools