1kmz

From Proteopedia

(Difference between revisions)

Current revision

MOLECULAR BASIS OF MITOMYCIN C RESICTANCE IN STREPTOMYCES: CRYSTAL STRUCTURES OF THE MRD PROTEIN WITH AND WITHOUT A DRUG DERIVATIVE

Structural highlights

1kmz is a 1 chain structure with sequence from Streptomyces lavendulae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O05205_STRLA

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

Mitomycin C (MC) is a potent anticancer agent. Streptomyces lavendulae, which produces MC, protects itself from the lethal effects of the drug by expressing several resistance proteins. One of them (MRD) binds MC and functions as a drug exporter. We report the crystal structure of MRD and its complex with an MC metabolite, 1,2-cis-1-hydroxy-2,7-diaminomitosene, at 1.5 A resolution. The drug is sandwiched by pi-stacking interactions of His-38 and Trp-108. MRD is a dimer. The betaalphabetabetabeta fold of the MRD molecule is reminiscent of methylmalonyl-CoA epimerase, bleomycin resistance proteins, glyoxalase I, and extradiol dioxygenases. The location of the binding site is identical to the ones in evolutionarily related enzymes, suggesting that the protein may have been recruited from a different metabolic pathway.

Molecular basis of mitomycin C resistance in streptomyces: structure and function of the MRD protein.,Martin TW, Dauter Z, Devedjiev Y, Sheffield P, Jelen F, He M, Sherman DH, Otlewski J, Derewenda ZS, Derewenda U Structure. 2002 Jul;10(7):933-42. PMID:12121648^[1]

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

References

↑ Martin TW, Dauter Z, Devedjiev Y, Sheffield P, Jelen F, He M, Sherman DH, Otlewski J, Derewenda ZS, Derewenda U. Molecular basis of mitomycin C resistance in streptomyces: structure and function of the MRD protein. Structure. 2002 Jul;10(7):933-42. PMID:12121648

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1kmz.png|left|200px]]
-<!--
+==MOLECULAR BASIS OF MITOMYCIN C RESICTANCE IN STREPTOMYCES: CRYSTAL STRUCTURES OF THE MRD PROTEIN WITH AND WITHOUT A DRUG DERIVATIVE==
-The line below this paragraph, containing "STRUCTURE_1kmz", creates the "Structure Box" on the page.
+<StructureSection load='1kmz' size='340' side='right'caption='[[1kmz]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1kmz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lavendulae Streptomyces lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KMZ FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</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=1kmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kmz OCA], [https://pdbe.org/1kmz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kmz RCSB], [https://www.ebi.ac.uk/pdbsum/1kmz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kmz ProSAT]</span></td></tr>
-{{STRUCTURE_1kmz|  PDB=1kmz  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/O05205_STRLA O05205_STRLA]
+== 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/km/1kmz_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1kmz ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Mitomycin C (MC) is a potent anticancer agent. Streptomyces lavendulae, which produces MC, protects itself from the lethal effects of the drug by expressing several resistance proteins. One of them (MRD) binds MC and functions as a drug exporter. We report the crystal structure of MRD and its complex with an MC metabolite, 1,2-cis-1-hydroxy-2,7-diaminomitosene, at 1.5 A resolution. The drug is sandwiched by pi-stacking interactions of His-38 and Trp-108. MRD is a dimer. The betaalphabetabetabeta fold of the MRD molecule is reminiscent of methylmalonyl-CoA epimerase, bleomycin resistance proteins, glyoxalase I, and extradiol dioxygenases. The location of the binding site is identical to the ones in evolutionarily related enzymes, suggesting that the protein may have been recruited from a different metabolic pathway.
-===MOLECULAR BASIS OF MITOMYCIN C RESICTANCE IN STREPTOMYCES: CRYSTAL STRUCTURES OF THE MRD PROTEIN WITH AND WITHOUT A DRUG DERIVATIVE===
+Molecular basis of mitomycin C resistance in streptomyces: structure and function of the MRD protein.,Martin TW, Dauter Z, Devedjiev Y, Sheffield P, Jelen F, He M, Sherman DH, Otlewski J, Derewenda ZS, Derewenda U Structure. 2002 Jul;10(7):933-42. PMID:12121648<ref>PMID:12121648</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12121648}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1kmz" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12121648 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12121648}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-KMZ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lavendulae Streptomyces lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KMZ OCA].
-==Reference==
-<ref group="xtra">PMID:12121648</ref><references group="xtra"/>
 [[Category: Streptomyces lavendulae]]
-[[Category: Dauter, Z.]]
+[[Category: Dauter Z]]
-[[Category: Derewenda, U.]]
+[[Category: Derewenda U]]
-[[Category: Derewenda, Z S.]]
+[[Category: Derewenda ZS]]
-[[Category: Devedjiev, Y.]]
+[[Category: Devedjiev Y]]
-[[Category: He, M.]]
+[[Category: He M]]
-[[Category: Jelen, F.]]
+[[Category: Jelen F]]
-[[Category: Martin, T W.]]
+[[Category: Martin TW]]
-[[Category: Otlewski, J.]]
+[[Category: Otlewski J]]
-[[Category: Sheffield, P.]]
+[[Category: Sheffield P]]
-[[Category: Sherman, D.]]
+[[Category: Sherman D]]
-[[Category: Anomalous diffraction]]
-[[Category: Antibiotic resistance]]
-[[Category: Crystal structure]]
-[[Category: Domain swapping]]
-[[Category: Mitomycin c]]
-[[Category: P-staking]]
-[[Category: Sad]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:05:06 2009''

1kmz

From Proteopedia

Current revision

MOLECULAR BASIS OF MITOMYCIN C RESICTANCE IN STREPTOMYCES: CRYSTAL STRUCTURES OF THE MRD PROTEIN WITH AND WITHOUT A DRUG DERIVATIVE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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