1noa: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(2 intermediate revisions by the same user not shown)
Line 3: Line 3:
<StructureSection load='1noa' size='340' side='right'caption='[[1noa]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='1noa' size='340' side='right'caption='[[1noa]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1noa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/'streptomyces_carzinostaticus' 'streptomyces carzinostaticus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NOA FirstGlance]. <br>
<table><tr><td colspan='2'>[[1noa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_carzinostaticus Streptomyces carzinostaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NOA FirstGlance]. <br>
</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=1noa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1noa OCA], [http://pdbe.org/1noa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1noa RCSB], [http://www.ebi.ac.uk/pdbsum/1noa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1noa ProSAT]</span></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]] 1.5&#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=1noa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1noa OCA], [https://pdbe.org/1noa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1noa RCSB], [https://www.ebi.ac.uk/pdbsum/1noa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1noa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NCZS_STRCZ NCZS_STRCZ]] NCS has antibiotic activity (for Gram-positive bacteria) and antitumor activity (for certain mouse tumors). NCS binds non-covalently to a chromophore which is the cytotoxic and mutagenic component of the antibiotic. The chromophore binds to DNA as a weak intercalator and causes single- and double-strand breaks.  
[https://www.uniprot.org/uniprot/NCZS_STRCZ NCZS_STRCZ] NCS has antibiotic activity (for Gram-positive bacteria) and antitumor activity (for certain mouse tumors). NCS binds non-covalently to a chromophore which is the cytotoxic and mutagenic component of the antibiotic. The chromophore binds to DNA as a weak intercalator and causes single- and double-strand breaks.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 13: Line 14:
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/no/1noa_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/no/1noa_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
Line 31: Line 32:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces carzinostaticus]]
[[Category: Streptomyces carzinostaticus]]
[[Category: Large Structures]]
[[Category: Teplyakov A]]
[[Category: Teplyakov, A]]
[[Category: Antibacterial protein]]

Latest revision as of 11:40, 6 November 2024

CRYSTAL STRUCTURE OF APO-NEOCARZINOSTATIN AT 0.15 NM RESOLUTIONCRYSTAL STRUCTURE OF APO-NEOCARZINOSTATIN AT 0.15 NM RESOLUTION

Structural highlights

1noa is a 1 chain structure with sequence from Streptomyces carzinostaticus. 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

NCZS_STRCZ NCS has antibiotic activity (for Gram-positive bacteria) and antitumor activity (for certain mouse tumors). NCS binds non-covalently to a chromophore which is the cytotoxic and mutagenic component of the antibiotic. The chromophore binds to DNA as a weak intercalator and causes single- and double-strand breaks.

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 three-dimensional structure of apo-neocarzinostatin, an antitumour antibiotic protein isolated from Streptomyces carzinostaticus, has been determined by X-ray diffraction at 0.15-nm resolution and refined to R = 17.2%. The crystal structure of neocarzinostatin is similar to that of the related proteins actinoxanthin and macromomycin. It is also in good agreement with the solution structure determined by NMR spectroscopy. The protein molecule consists of a seven-stranded antiparallel beta-sandwich and a smaller lobe formed by two beta-ribbons. A deep cleft between the two lobes is a putative chromophore binding site. Side chains of Trp39, Leu45, Phe52, Phe78 and the disulphide Cys37-Cys47 aligning the binding cleft in neocarzinostatin suggest the importance of hydrophobic interactions in stabilizing the chromophore molecule. Comparison of the atomic models of neocarzinostatin, actinoxanthin and macromomycin reveals functional residues which might determine specificity towards different chromophores.

Crystal structure of apo-neocarzinostatin at 0.15-nm resolution.,Teplyakov A, Obmolova G, Wilson K, Kuromizu K Eur J Biochem. 1993 Apr 15;213(2):737-41. PMID:8477746[1]

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

References

  1. Teplyakov A, Obmolova G, Wilson K, Kuromizu K. Crystal structure of apo-neocarzinostatin at 0.15-nm resolution. Eur J Biochem. 1993 Apr 15;213(2):737-41. PMID:8477746

1noa, resolution 1.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA